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Information on EC 2.4.1.222 - O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase and Organism(s) Mus musculus and UniProt Accession O09010
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2.4.1.222 O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferaseIUBMB Comments
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc and alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
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Word Map
- 2.4.1.222
- notch
- glycosyltransferases
- somite
- mesoderm
- n-glycans
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presomitic
- n-acetylglucosamine
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somitogenesis
- udp-n-acetylglucosamine
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galactosyltransferase
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delta1
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jagged1
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paraxial
- dll1
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delta-like
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bisect
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fucose-specific
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unsegmented
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o-fucosylation
- n-acetyllactosamine
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o-mannose
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glcnac-ts
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delta-notch
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n-acetylglucosaminylated
- pomgnt1s
- poly-n-acetyllactosamine
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o-fucosyltransferase
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tetraantennary
- gnt-ivs
-
o-mannosylated
- synthesis
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-acetylglucosaminyltransferase, lunatic fringe, radical fringe, manic fringe, beta1,3-n-acetylglucosaminyltransferase, beta-1,3-n-acetylglucosaminyltransferase, fringe protein, glycosyltransferase fringe, beta1,3-n-acetylglucosaminyltransferase-2, fringe glycosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminylferase, uridine diphosphoacetylglucosamine:fucosyglycoprotein beta1-3-
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beta1,3-acetylglucosaminyltransferase
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Fringe
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fringe beta1,3 N-acetylglucosaminyltransferase
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fringe glycosyltransferase
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LFNG
Lunatic Fringe
lunatic fringe glycosyltransferase
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Manic fringe
manic fringe glycosyltransferase
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O-fucose-beta1,3-N-acetylglucosaminyltransferase
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O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase
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radical fringe glycosyltransferase
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UDP-acetylglucosamine:fucosylglycoprotein
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UDP-D-GlcNAc:O-L-fucosylpeptide 3-beta-N-acetyl-D-glucosaminyltransferase
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UDP-GlcNAc:fucose beta1,3 N-acetylglucosaminyltransferase
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UDP-glucose:O-linked fucose beta1,3-glucosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:[protein with EGF-like domain]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine) 3-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc and alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
299203-70-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl-alpha-L-fucose + UDP-beta-D-GlcNAc
GlcNAc-beta-1,3-fucitol + p-nitrophenol + UDP
-
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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-
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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Fringe genes encode beta-1,3-N-acetyl-glucosaminyltransferases, which elongate O-fucose on the EGF repeat of Notch and its ligands
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-
?
additional information
?
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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?
additional information
?
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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-
?
additional information
?
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Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose
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-
?
additional information
?
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Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose
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?
additional information
?
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Fringe elongates O-fucose residues on EGF-like repeat 4 and 5 of Notch3. Fringe plays a role in CADASIL pathophysiology
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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LFNG, Lunatic Fringe, and MFNG, Manic Fringe, transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF-like repeats of NOTCH receptors
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?
additional information
?
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O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
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?
additional information
?
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the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. Lfng inhibits activation of Notch1 and Notch4 in basal cells of the mouse prostate gland while enhancing Notch3 activation
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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-
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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Fringe genes encode beta-1,3-N-acetyl-glucosaminyltransferases, which elongate O-fucose on the EGF repeat of Notch and its ligands
-
-
?
additional information
?
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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-
?
additional information
?
-
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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?
additional information
?
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Fringe elongates O-fucose residues on EGF-like repeat 4 and 5 of Notch3. Fringe plays a role in CADASIL pathophysiology
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-
?
additional information
?
-
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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-
?
additional information
?
-
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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LFNG, Lunatic Fringe, and MFNG, Manic Fringe, transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF-like repeats of NOTCH receptors
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?
additional information
?
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O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
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-
?
additional information
?
-
the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. Lfng inhibits activation of Notch1 and Notch4 in basal cells of the mouse prostate gland while enhancing Notch3 activation
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
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Gal is required for the enhancement of Notch signaling by LFNG, whereas Gal inhibits the enhancement of DLL1-induced NOTCH signaling by MFNG
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
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Gal is required for the enhancement of Notch signaling by LFNG, whereas Gal inhibits the enhancement of DLL1-induced NOTCH signaling by MFNG
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of Lfng in the prostate is relatively low compared with manic fringe and radical fringe but more restricted to basal epithelium
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Lfng continues to be highly expressed after thymus-seeding progenitors develop into T cell-committed DN2 (CD117+ CD25+) and then DN3a (CD117- CD25+) pro-T cells, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
metabolism
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O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255. The structure GlcNAcbeta1-3Fucalpha1-OSer/Thr can be further elongated in mammals to the tetrasaccharide by sequential action of a beta1-4galactosyltransferase and an alpha2-3 or alpha2-6sialyltransferase
physiological function
additional information
malfunction
deletion of gene lfng impairs myofibroblast differentiation and alveogenesis, alveolar developmental defect in Lfng mutants with altered elastogenesis and collagen deposition in Lfng mutant lungs, phenotype, overview
malfunction
loss of the DSL protein DLL3 in the mouse results in severe somite patterning defects, which are virtually indistinguishable from the defects in mice that lack the enzyme lunatic fringe. Embryos double homozygous for null mutations in Dll3 and Lfng are phenotypically indistinguishable from the single mutants supporting a potential common function. Mutation of the O-fucosylation sites in DLL3 does not disrupt the interaction of DLL3 with LFNG or full length Notch1or DLL1, and O-fucosylation-deficient DLL3 can still inhibit Notch in cis in vitro. In contrast to wild type DLL3, O-fucosylation-deficient DLL3 cannot compensate for the loss of endogenous DLL3 during somitogenesis in the embryo
physiological function
Lunatic Fringe, Lfng, is a beta1-3 N-acetylglucosamine transferase that modifies Notch receptors to facilitate their activation by Delta-like (Dll1/4) ligands, Lfng functions to enhance Notch-dependent induction of myofibroblast differentiation during embryonic lung development in the mouse
physiological function
enzyme lunatic fringe is a glycosyltransferase involved in modifying Notch signaling. modification of DLL3 by O-linked fucose via the action of enzyme lunatic fringe is essential for its function during somitogenesis
malfunction
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eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters the activity in cell-based Notch signaling assays. EGF 12 is part of the ligand-binding region of Notch, a mouse line carrying a point mutation in the O-fucosylation site of EGF 12 in endogenous Notch1 shows loss of this site which results in a mild Notch phenotype with defects in T cell development
malfunction
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impact of Lfng deficiency on beta-selection, decreasing Lfng expression during the DN3-DP transition minimizes the potent leukemogenic potential of Notch1 signaling
malfunction
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Lfng depletion does not affect the balance between neuronally committed cells and selfrenewing progenitors, irrespective of the cell density of Lfng-depleted cells, and causes no obvious defects in brain development, but in vivo overexpression of Lfng shows that it strongly augments Notch signaling mediated by Delta-like 1 but not Jagged 1, phenotypes, overview
malfunction
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Lfng modification of EGF12 in the Notch1 ligand-binding domain contributes to, but is not solely responsible for, the cell-nonautonomous inhibition of T cell development caused by transgenic Lfng expression in double-positive thymocytes. O-fucose site in the Notch1 ligand binding domain is partly responsible for the effects of Lfng overexpression
malfunction
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the NOTCH signaling effect through MFNG is abolished by a DDD to DDA mutation in MFNG that inactivates its GlcNAc transferase activity
malfunction
deletion of Lfng in mice causes altered Notch activation in the prostate, associated with elevated accumulation of Notch1, Notch2, and Notch4 intracellular domains, decreased levels of the putative Notch3 intracellular fragment, as well as increased expression of Hes1, Hes5, and Hey2. Loss of Lfng results in expansion of the basal layer, increased proliferation of both luminal and basal cells, and ultimately, prostatic intraepithelial neoplasia. The Lfng-null prostate shows down-regulation of prostatic tumor suppressor gene NKX3.1 and increased androgen receptor expression. Deletion of Lfng caused dysregulation of Notch signaling in the prostate. Increased epithelial proliferation and prostatic intraepithelial neoplasia in the Lfng-null mutant gland
physiological function
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isoform manic fringe expression is not required for embryonic development. Despite significant overlap in expression patterns, there are no obvious synergistic defects in mice in the absence of two, or all three, fringe genes during development of the axial skeleton, limbs, hindbrain, and cranial nerves
physiological function
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isoforms lunatic fringe and manic fringe cooperatively enhance the Delta-like-1-Notch2 interaction to promote splenic marginal zone B cell development
physiological function
-
Fringe proteins are glycosyltransferases that add N-acetylglucosamine to O-fucose moieties to the extracellular domains of Notch receptors. In the immune system, Lunatic Fringe, Lfng, plays a key role in the early stages of T-lymphocyte development, critically enhancing DL4/Notch1-dependent suppression of alternative B-lineage potential and promoting T-lineage specification. Furthermore, Lfng and Manic Fringe cooperatively enhance DL1-induced Notch2 activation to promote marginal zone B-cell development. Lfng enhances Notch1 activation by Delta-like 4 to promote Notch1-dependent T-lineage commitment of thymus-seeding progenitors. Lfng temporally sustains Delta-like-induced Notch1 signaling to prolong proliferative self-renewal of pre-DP thymocytes. Pre-TCR signaling greatly augments Notch trophic functions to promote robust proliferation of pre-double positive progenitors. In the absence of DL/Notch signaling, pre-TCR expressing progenitors rapidly atrophy and differentiate into double positive thymocytes
physiological function
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LFNG and MFNG are both required for the optimal generation of MZB cells in spleen consistent with a synergistic action on Notch. Differential modification of EGF repeats on Notch by LFNG versus MFNG: MFNG promotes DLL1-induced NOTCH signaling better in the absence of Gal than in its presence, the effect is reversed in Lec8 cells corrected by expression of a UDP-Gal transporter cDNA. MFNG activity is required to enhance DLL1-induced Notch signaling in Lec8 cells. In co-culture Notch signaling assays, LFNG generally enhances DLL1-induced Notch signaling, but not in either Lec8 or Lec20 CHO mutants lacking Gal on O-fucose glycans. LFNG generally inhibits JAG1-induced Notch signaling, but in mutant CHO cells that do not add galactose to the GlcNAc transferred by Fringe, JAG1-induced Notch signaling is not inhibited by LFNG or MFNG, roles for Gal in LFNG and MFNG modulation of DLL1-induced Notch signaling in CHO cells, overview
physiological function
-
Notch signaling is essential for the self-renewal of mammalian neural progenitor cells. A variety of mechanisms modulate Notch signaling to balance the self-renewal and differentiation of progenitor cells. Fringe is a major Notch regulator and promotes or suppresses Notch signaling, depending on the Notch ligands. Lfng potentiates Notch signaling cell autonomously in neural progenitor cells of developinmg brain. Lfng and Notch intracellular domain affect embryonic self-renewing progenitor cell identity and cell proliferation in a similar way
physiological function
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Notch1 activation by Delta-like Notch ligands is essential to induce T cell commitment and to suppress B cell development from thymus-seeding progenitors. Thymus-seeding progenitor competition for Delta-like ligand DL4 is critically regulated by Lunatic Fringe, which glycosylates epidermal growth factor repeats in the Notch1 extracellular domain to enhance binding avidity for Delta-like ligands. Notch1 activation is also essential for the process of beta-selection, which drives TCRbeta+ CD4/CD8 double-negative 3 precursors to proliferate and generate a large pool of CD4/CD8 double-positive thymocytes. Lunatic Fringe enhances competition for delta-like Notch ligands but does not overcome defective pre-TCR signaling during thymocyte beta-selection in vivo, importance of Lfng-Notch1 interactions in regulating competition of preselection and postselection DN3 thymocytes for DL ligands in vivo, overview. Transgenic Lfng confers a competitive advantage to wild-type but not Rag2-/- DN3 thymocytes. Lfng improves the competitive fitness of Lck-deficient and Ptcra-deficient DN3beta thymocytes
physiological function
-
the O-fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellulr domain. O-GlcNAc modification, a third form of O-glycosylation, occurs on EGF repeats, on hydroxy amino acids between the fifth and sixth conserved Cys of an EGF repeat. Similar to O-fucosylation, the major effect of Fringe-mediated O-fucose elongation appears to be modulation of Notch-ligand binding, whereby Delta activation of Notch is potentiated, while signaling via Serrate is inhibited. Mammalian Fringe modification also alters ligand binding. Elongation beyond GlcNAc to the trisaccharide (Galbeta1-4GlcNAcbeta1-3-Fucosealpha1-O-Ser/Thr) is necessary to see a Fringe effect in a mammalian cell system
physiological function
fringe genes code for O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferases that can add N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. This modification modulates specificity and sensitivity of Notch receptors for different ligands. Therefore, fringes are powerful regulators of ligand-mediated Notch signaling. Tumor-suppressive activity of lunatic fringe in prostate through differential modulation of Notch receptor activation. The enzyme plays a critical role in regulation of prostate epithelial differentiation and proliferation, as well as in prostate tumor suppression
additional information
-
Fringe elongation to the GlcNAc-beta1,3-fucose causes a significant conformational shift of several residues within the O-fucose consensus region. This may provide a mechanism for how Fringe modification indirectly exerts its effects on Notch activity at EGF 12
additional information
-
Lfng overexpression enhances proliferative expansion of DN3 and DN4 thymocytes in response to Delta-like ligands in vitro. Lfng overexpression augments binding of Delta-like 1 and Delta-like 4 by double negative and double positive thymocytes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LFNG_MOUSE
378
1
41952
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour diffusion method. Abolishing the glycosylation sites by site-directed mutagenesis was necessary in order to obtain orthorhombic crystals that diffracted to 1.8 A resolution. Crystals belonged to space group P2(1)2(1)2. The unit-cell parameters (a = 162.6, b = 41.4, c = 38.8 A) are consistent with the presence of one molecule in the asymmetric unit
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D288A
active site mutant to short loop side of residue D289, activity too low to measure
G334H
donor specificity mutant, 94.6% of wild-type UDP-beta-D-GlcNAc utilization, 78.0% of wild-type UDP-Glc utilization
H313A
donor specificity mutant, 6.2% of wild-type UDP-beta-D-GlcNAc utilization, 75.9% of wild-type UDP-Glc utilization
H313A/G334H
donor specificity mutant, 3.1% of wild-type UDP-beta-D-GlcNAc utilization, 34.7% of wild-type UDP-Glc utilization
L314R
donor specificity mutant, 21.7% of wild-type UDP-beta-D-GlcNAc utilization, 119.5% of wild-type UDP-Glc utilization
S312T
donor specificity mutant, 1.9% of wild-type UDP-beta-D-GlcNAc utilization, 18.1% of wild-type UDP-Glc utilization
additional information
additional information
-
a DDD to DDA mutation inactivates MFNG GlcNAc transferase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of Flag-tagged DLL3 and HA-tagged LFNG in CHO cells, the two proteins coprecipitate
catalytic domain of murine Manic Fringe is expressed in the baculovirus/insect-cell system as a secreted protein
genes lfng and mfng, expression in wild-type CHO cells, in Lec1.3C, Lec2.6A, Lec8.3D, and Lec20.15C CHO glycosylation mutant lines, and in Lec8 and Lec20 CHO mutant lines
-
mouse FRINGE coding sequences are ligated into pcDNA3 for transfection of NIH3T3 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jinek, M.; Conti, E.
Eukaryotic expression, purification, crystallization and preliminary X-ray analysis of murine Manic Fringe
Acta Crystallogr. Sect. F
62
774-777
2006
Mus musculus (O09008), Mus musculus
Arboleda-Velasquez, J.F.; Rampal, R.; Fung, E.; Darland, D.C.; Liu, M.; Martinez, M.C.; Donahue, C.P.; Navarro-Gonzalez, M.F.; Libby, P.; DAmore, P.A.; Aikawa, M.; Haltiwanger, R.S.; Kosik, K.S.
CADASIL mutations impair Notch3 glycosylation by Fringe
Hum. Mol. Genet.
14
1631-1639
2005
Mus musculus
Jinek, M.; Chen, Y.W.; Clausen, H.; Cohen, S.M.; Conti, E.
Structural insights into the Notch-modifying glycosyltransferase Fringe
Nat. Struct. Mol. Biol.
13
945-946
2006
Mus musculus (O09008), Mus musculus
Shifley, E.T.; Cole, S.E.
Lunatic fringe protein processing by proprotein convertases may contribute to the short protein half-life in the segmentation clock
Biochim. Biophys. Acta
1783
2384-2390
2008
Mus musculus
Shifley, E.T.; Vanhorn, K.M.; Perez-Balaguer, A.; Franklin, J.D.; Weinstein, M.; Cole, S.E.
Oscillatory lunatic fringe activity is crucial for segmentation of the anterior but not posterior skeleton
Development
135
899-908
2008
Mus musculus
Moran, J.L.; Shifley, E.T.; Levorse, J.M.; Mani, S.; Ostmann, K.; Perez-Balaguer, A.; Walker, D.M.; Vogt, T.F.; Cole, S.E.
Manic fringe is not required for embryonic development, and fringe family members do not exhibit redundant functions in the axial skeleton, limb, or hindbrain
Dev. Dyn.
238
1803-1812
2009
Mus musculus
Tan, J.B.; Xu, K.; Cretegny, K.; Visan, I.; Yuan, J.S.; Egan, S.E.; Guidos, C.J.
Lunatic and manic fringe cooperatively enhance marginal zone B cell precursor competition for delta-like 1 in splenic endothelial niches
Immunity
30
254-263
2009
Mus musculus
Luther, K.B.; Schindelin, H.; Haltiwanger, R.S.
Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants
J. Biol. Chem.
284
3294-3305
2009
Mus musculus (O09008)
Xu, K.; Nieuwenhuis, E.; Cohen, B.; Wang, W.; Canty, A.; Danska, J.; Coultas, L.; Rossant, J.; Wu, M.; Piscione, T.; Nagy, A.; Gossler, A.; Hicks, G.; Hui, C.; Henkelman, R.; Yu, L.; Sled, J.; Gridley, T.; Egan, S.
Lunatic Fringe-mediated Notch signaling is required for lung alveogenesis
Am. J. Physiol. Lung Cell Mol. Physiol.
298
L45-L56
2010
Mus musculus (O09010)
Yuan, J.S.; Tan, J.B.; Visan, I.; Matei, I.R.; Urbanellis, P.; Xu, K.; Danska, J.S.; Egan, S.E.; Guidos, C.J.
Lunatic Fringe prolongs Delta/Notch-induced self-renewal of committed alphabeta T-cell progenitors
Blood
117
1184-1195
2011
Mus musculus
Rana, N.A.; Haltiwanger, R.S.
Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
Curr. Opin. Struct. Biol.
21
583-589
2011
Drosophila melanogaster, Mus musculus
Hou, X.; Tashima, Y.; Stanley, P.
Galactose differentially modulates Lunatic and Manic Fringe effects on Delta1-induced NOTCH signaling
J. Biol. Chem.
287
474-483
2012
Mus musculus
Visan, I.; Yuan, J.S.; Liu, Y.; Stanley, P.; Guidos, C.J.
Lunatic Fringe enhances competition for delta-like Notch ligands but does not overcome defective pre-TCR signaling during thymocyte beta-selection in vivo
J. Immunol.
185
4609-4617
2010
Mus musculus
Kato, T.M.; Kawaguchi, A.; Kosodo, Y.; Niwa, H.; Matsuzaki, F.
Lunatic fringe potentiates Notch signaling in the developing brain
Mol. Cell. Neurosci.
45
12-25
2010
Mus musculus
Zhang, S.; Chung, W.C.; Wu, G.; Egan, S.E.; Xu, K.
Tumor-suppressive activity of lunatic fringe in prostate through differential modulation of Notch receptor activation
Neoplasia
16
158-167
2014
Mus musculus (O09008), Homo sapiens (Q8NES3), Homo sapiens
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