BRENDA - Enzyme Database

Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells

Liu, G.H.; Gerace, L.; PLoS ONE 4, e7031 (2009)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.4
V5-tagged lipin-1alpha, lipin-1beta, lipin-2 and lipin-3 expression vectors. HEK-293A cells transfected with plasmids expressing V5-tagged proteins. HeLa cells transfected with expression plasmids for V5-lipin-1beta and CFP-SUMO-1 or their mutants. SH-SY5Y cells stably expressing pcDNA3, lipin-1alpha-V5 or lipin-1alpha-K566R/K596R-V5. Cerebrocortical neurons from embryonic day 17 rat embryos transfected either with V5-tagged lipin-1alpha or lipin-1beta, or with the corresponding double sumoylation site mutants
Mus musculus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.4
D679E
mutation in lipin-1alpha, does not lead to a diminished sumoylation
Mus musculus
3.1.3.4
G84R
mutation in lipin-1alpha, does not lead to a diminished sumoylation
Mus musculus
3.1.3.4
K566R/K596R
blocks lipin-1alpha sumoylation. In embryonic cortical neurons or SH-SY5Y clones, almost completely loses its nuclear localization compared to wild-type, although its cytoplasmic localization remains unchanged. Retains Mg2+-dependent phosphatase activity for phosphatidic acid (C8), but not for lysophosphatidic acid (C18:1)
Mus musculus
3.1.3.4
K599R/K626R
lipin-1beta mutant, is not modified by SUMO-1 in an in vitro sumoylation reaction
Mus musculus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
additional information
in embryonic cortical neurons, lipin-1beta shows exclusively cytoplasmic localization. In SH-SY5Y clones, ectopic lipin-1a exhibits both nuclear and cytosolic localization, with a higher concentration in the nucleus, whereas lipin-1alpha is concentrated in the cytoplasm in HEK-93A cells. Sumoylation facilitates the nuclear localization and transcriptional coactivator behavior of lipin-1alpha in embryonic cortical neurons
Mus musculus
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
assay buffer
Mus musculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.4
Mus musculus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
3.1.3.4
V5-tagged proteins immunopurified
Mus musculus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.4
brain
lipin-1, whereas lipin-1alpha is the predominant form
Mus musculus
-
3.1.3.4
liver
lipin-1
Mus musculus
-
3.1.3.4
muscle
highest level of lipin-1
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
lysophosphatidic acid + H2O
-
710376
Mus musculus
monoacylglycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
710376
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
V5-tagged lipin-1alpha, lipin-1beta, lipin-2 and lipin-3 expression vectors. HEK-293A cells transfected with plasmids expressing V5-tagged proteins. HeLa cells transfected with expression plasmids for V5-lipin-1beta and CFP-SUMO-1 or their mutants. SH-SY5Y cells stably expressing pcDNA3, lipin-1alpha-V5 or lipin-1alpha-K566R/K596R-V5. Cerebrocortical neurons from embryonic day 17 rat embryos transfected either with V5-tagged lipin-1alpha or lipin-1beta, or with the corresponding double sumoylation site mutants
Mus musculus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.4
D679E
mutation in lipin-1alpha, does not lead to a diminished sumoylation
Mus musculus
3.1.3.4
G84R
mutation in lipin-1alpha, does not lead to a diminished sumoylation
Mus musculus
3.1.3.4
K566R/K596R
blocks lipin-1alpha sumoylation. In embryonic cortical neurons or SH-SY5Y clones, almost completely loses its nuclear localization compared to wild-type, although its cytoplasmic localization remains unchanged. Retains Mg2+-dependent phosphatase activity for phosphatidic acid (C8), but not for lysophosphatidic acid (C18:1)
Mus musculus
3.1.3.4
K599R/K626R
lipin-1beta mutant, is not modified by SUMO-1 in an in vitro sumoylation reaction
Mus musculus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
additional information
in embryonic cortical neurons, lipin-1beta shows exclusively cytoplasmic localization. In SH-SY5Y clones, ectopic lipin-1a exhibits both nuclear and cytosolic localization, with a higher concentration in the nucleus, whereas lipin-1alpha is concentrated in the cytoplasm in HEK-93A cells. Sumoylation facilitates the nuclear localization and transcriptional coactivator behavior of lipin-1alpha in embryonic cortical neurons
Mus musculus
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
assay buffer
Mus musculus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
V5-tagged proteins immunopurified
Mus musculus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.4
brain
lipin-1, whereas lipin-1alpha is the predominant form
Mus musculus
-
3.1.3.4
liver
lipin-1
Mus musculus
-
3.1.3.4
muscle
highest level of lipin-1
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
lysophosphatidic acid + H2O
-
710376
Mus musculus
monoacylglycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
710376
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
3.1.3.4
malfunction
nuclear localization is abrogated by mutating the consensus sumyolation motifs. Sumoylation site mutant of lipin-1alpha loses the capacity to coactivate the transcriptional (co-) activators PGC-1alpha and MEF2, consistent with its nuclear exclusion
Mus musculus
3.1.3.4
physiological function
lipin-1alpha may act as a sumoylation-regulated transcriptional coactivator in brain. Sumoylated forms of lipin-1 in muscle and liver are only marginally present. Lipin-1 (including both the alpha and beta isoforms) is modified by sumoylation at two consensus sumoylation sites, is sumoylated at relatively high levels in brain. No sumoylation of the related proteins lipin-2 and lipin-3
Mus musculus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.1.3.4
malfunction
nuclear localization is abrogated by mutating the consensus sumyolation motifs. Sumoylation site mutant of lipin-1alpha loses the capacity to coactivate the transcriptional (co-) activators PGC-1alpha and MEF2, consistent with its nuclear exclusion
Mus musculus
3.1.3.4
physiological function
lipin-1alpha may act as a sumoylation-regulated transcriptional coactivator in brain. Sumoylated forms of lipin-1 in muscle and liver are only marginally present. Lipin-1 (including both the alpha and beta isoforms) is modified by sumoylation at two consensus sumoylation sites, is sumoylated at relatively high levels in brain. No sumoylation of the related proteins lipin-2 and lipin-3
Mus musculus