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Information on EC 3.6.5.5 - dynamin GTPase and Organism(s) Mus musculus and UniProt Accession P39054
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3.6.5.5 dynamin GTPaseIUBMB Comments
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
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Word Map
- 3.6.5.5
-
endocytosis
- gtpases
-
endocytic
- clathrin
- actin
- synaptic
-
clathrin-mediated
- endosomes
-
dominant-negative
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clathrin-coated
-
mitofusins
- cytoskeleton
- dynasore
- pi
- tubule
-
scission
-
mitophagy
-
constrict
- microtubule
- transferrin
-
receptor-mediated
- adaptor
- synapses
-
presynaptic
- myopathy
- rab5
- pink1
-
caveolae
-
brachytherapy
-
gtp-binding
- src
-
mechanochemical
-
clathrin-independent
- eps15
- caveolin-1
-
macropinocytosis
- parkin
- charcot-marie-tooth
-
cristae
-
pleckstrin
-
invagination
- arf6
- agriculture
- arrestins
- medicine
-
pten-induced
-
n-wasp
-
dosimetric
- cortactin
-
dose-volume
- grb2
- beta-arrestins
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
dynamin, dynamin-related protein 1, dynamin 2, d100, dynamin-2, dynamin 1, dynamin i, optic atrophy 1, dynamin-1, gtpase dynamin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B-dynamin
-
-
-
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D100
-
-
-
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Dynamin BREDNM19
-
-
-
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dynamin GTPase
Dynamin UDNM
-
-
-
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Dynamin, brain
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-
-
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Dynamin, testicular
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-
-
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GTP phosphohydrolase
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-
-
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GTPase
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-
-
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guanine triphosphatase
-
-
-
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guanosine 5'-triphosphatase
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-
-
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guanosine triphosphatase
-
-
-
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phosphatase, guanosine tri-
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-
-
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ribosomal GTPase
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-
-
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Shibire protein
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-
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T-dynamin
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (vesicle-releasing)
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
CAS REGISTRY NUMBER
COMMENTARY
9059-32-9
-
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
additional information
?
-
dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells, dynamin 2 is involved in PI(4,5)P2-induced actin polymerisation during phagocytosis
-
-
?
additional information
?
-
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dynamin is required for budding of clathrin-coated vesicles from the plasma membrane, functional dynamin is required for muramyl dipeptide-induced internalization and signaling
-
-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
-
-
?
additional information
?
-
-
in addition to the GTPase domain, neurolastin also has an E3 ubiquitin ligase domain, the enzyme shows E3 ligase activity in an in vitro ubiquitination assay
-
-
?
additional information
?
-
neurolastin exhibits both GTPase and E3 ligase activities
-
-
-
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
additional information
?
-
dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells, dynamin 2 is involved in PI(4,5)P2-induced actin polymerisation during phagocytosis
-
-
?
additional information
?
-
-
dynamin is required for budding of clathrin-coated vesicles from the plasma membrane, functional dynamin is required for muramyl dipeptide-induced internalization and signaling
-
-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
-
-
?
additional information
?
-
-
in addition to the GTPase domain, neurolastin also has an E3 ubiquitin ligase domain, the enzyme shows E3 ligase activity in an in vitro ubiquitination assay
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-2-(aminomethyl)-N,N-diethyl-1-phenyl-cyclopropane-1-carboxamide
-
milnacipran
(3S-trans)-3-((1,3-benzodioxol-5-yloxy)methyl)-4-(4-fluorophenyl)-piperidine
-
paroxetine
1-[3-(dimethylamino)propyl]-1-(4-fluorophenyl)-1,3-dihydro[2]benzofuran-5-carbonitrile
-
citalopram
3-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylidene)-N-methyl-1-propanamine
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nortriptyline
3-(2-chloro-10H-phenothiazin-10-yl)-N,N-dimethyl-propan-1-amine
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chlorpromazine
3-(5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
-
imipramine
3-(9-chloro-5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
-
clomipramine
4-[4-(4-chlorophenyl)-4-hydroxy-1-piperidyl]-1-(4-fluorophenyl)-butan-1-one
-
haloperidol
fluvoxamine
-
a noncompetitive inhibitor of dynamin I with respect to GTP and a competitive inhibitor with respect to L-phosphatidylserine
sertraline
-
a mixed type inhibitor with respect to both GTP and L-phosphatidylserine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-phosphatidylserine
-
binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
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phosphatidylinositol-4,5-bisphosphate
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binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
additional information
-
robust stimulation of dynamin's GTPase activity upon polymerization
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(1R,2R)-2-(aminomethyl)-N,N-diethyl-1-phenyl-cyclopropane-1-carboxamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0234
(3S-trans)-3-((1,3-benzodioxol-5-yloxy)methyl)-4-(4-fluorophenyl)-piperidine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
1,2,3,4,10,14b-hexahydro-2-methyldibenzo[c,f]pyrazino[1,2-a]azepine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
1-[3-(dimethylamino)propyl]-1-(4-fluorophenyl)-1,3-dihydro[2]benzofuran-5-carbonitrile
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
10,11-dihydro-5-[3-(methylamino)propyl]-5H-dibenz[b,f]azepine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0372
2-[(8-chlorodibenzo[b,f]thiepin-10-yl)oxy]-N,N-dimethylethanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.064
3-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylidene)-N-methyl-1-propanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0472
3-(2-chloro-10H-phenothiazin-10-yl)-N,N-dimethyl-propan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
3-(5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0299
3-(9-chloro-5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
4-[4-(4-chlorophenyl)-4-hydroxy-1-piperidyl]-1-(4-fluorophenyl)-butan-1-one
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
5H-dibenz[b,f]azepine-5-carboxamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
methyl 2-phenyl-2-(2-piperidyl)acetate
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0241
myristyl trimethyl ammonium bromide
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
N-(2-diethylaminoethyl)-2-methoxy-5-methylsulfonyl-benzamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0334
N-methyl-3-phenyl-3-[4-(trifluoromethyl)phenoxy]-propan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0211
N-methyl-9,10-ethanoanthracene-9(10H)-propanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
N-[(1-ethylpyrrolidin-2-yl)methyl]-2-methoxy-5-sulfamoyl-benzamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
isozyme dynamin 2 is expressed ubiquitously. Isozyme dynamin 3 is found predominantly in the brain (at much lower levels than dynamin 1) and testis, and at lower levels in some tissues, such as the lung
-
neuronal dynamin I plays a critical role in the recycling of synaptic vesicles, and thus in nervous system function
-
isozyme dynamin2, isozyme dynamin 1 is selectively expressed at high levels in neurons and is generally not present in non-neuronal tissues
primary hippocampal neurons, isolated from P0-P1 pups of transgenic animals expressing HA-tagged enzyme
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
dynamin is a general component of clathrin-coated endocytic pits
-
neurolastin is peripherally associated with membranes via its C-terminus and localizes to endocytic vesicles
-
neurolastin is peripherally associated with membranes via its C-terminus but seems to contains two transmembrane segments
neurolastin is developmentally regulated and present on mitochondria. Neurolastin also localizes to mitochondria in transgenic HeLa cells, cultured neurons, and brain tissue. The mitochondrial localization of neurolastin depends upon an N-terminal mitochondrial targeting sequence. Neurolastin is imported into the mitochondrial intermembrane space. Although neurolastin is only partially mitochondrially localized at steady state, it displays increased translocation to mitochondria in response to neuronal stress and mitochondrial fragmentation
additional information
determination of colocalization of recominant GFP-tagged enzyme with mitochondria in neurons and brains of transgenic mice. Immunohistochemic analysis
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
structure-function relationship, overview. The C-terminal Pro-rich region, PRD, contains an array of PXXP amino acid motifs, which interact with many SH3 domain-containing proteins to localize dynamin at endocytic sites and coordinate dynamin's function with these other factors during endocytosis. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
evolution
-
neurolastin is a unique dynamin family GTPase with a RING domain, sequence analysis shows that neurolastin has a C3HC4-type RING domain and key residues important for zinc coordination are conserved
evolution
the OPA1 gene encodes a mitochondrial protein that belongs to the dynamins family, with which it shares three conserved regions: a GTPase domain, a middle domain, and a GTPase effector domain (GED) containing a coiled-coil domain (CC2), overview
evolution
neurolastin is a dynamin family GTPase. It also contains a RING domain and exhibits both GTPase and E3 ligase activities
malfunction
-
dynamin mutants with impaired GTP binding and/or hydrolysis cycles have dominant-negative effects on endocytosis. Also PH-domain mutants that impair phosphoinositide binding exert dominant-negative effects on clathrin-mediated endocytosis. Dynamin lacking the PRD cannot rescue endocytic defects in dynamin-knockout fibroblasts
malfunction
R386G mutation in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids. Vesicle formed in endocytosis are smaller in enzyme mutant R386G cells compared to wild-type
malfunction
silencing of OPA1 reduces induced lipolysis within the differentiated adipocytes
malfunction
neurolastin knockout animals have fewer dendritic spines and exhibit a reduction in functional synapses
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
the small group of dynamin-like GTPases as central regulators of mitochondrial morphology and cristae remodeling, apoptosis, calcium signaling, and metabolism
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Diverse roles for dynamin-like proteins at membrane interfaces, overview. Dynamin is also implicated in some clathrin-independent endocytic pathways, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamin interacts both directly and indirectly with the cytoskeleton, overview. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis
physiological function
-
dynamin family GTPases are key membrane remodeling mechanoenzymes. Neurolastin, a dynamin family GTPase, regulates excitatory synapses and spine density. Neurolastin affects endosome size via its RING domain. It is important for excitatory neurotransmission
physiological function
dynamin plays an important role in membrane fission during endocytosis. The dynammin GTPase is important for dynamin oligomer complex dissociation in absence of lipids
physiological function
OPA1 mediates adrenergic control of lipolysis by functioning as a cytosolic A-kinase anchoring protein (AKAP), on the hemimembrane that envelops the lipid droplet. Enzyme is OPA1 a regulator of mitochondrial inner membrane fusion and cristae remodeling, role of OPA1 in mtDNA maintenance and mitochondrial energetics. Enzyme regulation, m-AAA protease controls both cleavage and turnover of OPA1, OMA1 is activated upon attenuation of its proteolytic degradation, overview
physiological function
neurolastin, a dynamin family GTPase, translocates to mitochondria upon neuronal stress and alters mitochondrial morphology in vivo. It is specifically expressed in the brain and is important for synaptic transmission
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). DYN2_MOUSE
870
0
98145
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
dynamin 2 interacts with complexin in a GST-pulldown assay, it is identified by SDS-PAGE and Westernblotting and by mass spectroscopy
95000
-
identified in immunoprecipitation experiments by MS/MS sequence analysis
additional information
additional information
anti-mOPA1 antibodies detect a double band of approximately 90 and 80 kDa
additional information
-
anti-mOPA1 antibodies detect a double band of approximately 90 and 80 kDa
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
-
a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
additional information
additional information
-
structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
the enzyme's middle domain is involved in the formation of functional oligomers. Wild-type enzyme forms oligomers, while enzyme mutant R386G prefers to form monomers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ubiquitination
ubiquitin-mediated regulation of dynamin GTPases serves as a quality control mechanism for maintaining mitochondrial dynamics
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D273A
OPA1 missense mutation associated with autosomal dominant optic atrophy
E270K
OPA1 missense mutation associated with autosomal dominant optic atrophy
GST-Dyn1-C
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
GST-Dyn1-N
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
GST-Dyn1-PRD
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
OPA1Q285STOP
naturally occuring mutation, heterozygous mutant mice, carrying either a premature stop codon (OPA1Q285STOP/+) or an in-frame deletion of 27 amino acids (OPA1Q329-355del/+) in the GTPase domain, are based on haploinsufficiency since both models show a 50% reduction in OPA1 protein expression
Q329-355del
naturally occuring mutation, heterozygous mutant mice, carrying either a premature stop codon (OPA1Q285STOP/+) or an in-frame deletion of 27 amino acids (OPA1Q329-355del/+) in the GTPase domain, are based on haploinsufficiency since both models show a 50% reduction in OPA1 protein expression
R386G
site-directed mutagenesis, replacement of Arg386 with Gly in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids, while in presence of phosphatidylserine liposomes, the intermolecular interactions of dynamin 1 are not affected. The mutant is a monomer with reduced GTPase activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione S-transferase dynamin-1 fusion constructs are expressed in Escherichia coli BL21 cells, the proteins are purified using glutathione-Sepharose 4B beads
-
TALON metal affinity resin column chromatography and MonoQ column chroamtography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Rnf112, recombinant expression of C-terminally HA-tagged enzyme in transgenic C83S/C103S mutant mice and in HeLa cells, and of GFP-tagged enzyme from pEGFP-N1 vector in transgenic mice
recombinant expression of HA-tagged neurolastin in HEK cells, recombinant expression of GST-tagged wild-type and mutant enzymes in HeLa cells
-
recombinant expression of His6-tagged or FLAG-tagged wild-type and mutant enzymes in HeLa cells
the full-length mouse dynamin-1 cDNA isolated from retina is subcloned into the pGEX-2TK vector, the construct is used to generate three different dynamin-1 domain constructs, the N-terminal domain, aa 1-520, the proline-rich domain, aa 750-814, and the C-terminal domain, aa 521-814
-
wild-type mOPA1 and its mutants are subcloned into the mammalian expression vector pCNX2 for transfection of COS-7 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
dynamin-1 interacts with TULP1, TULP1 is a photoreceptor-specific protein that is mutated in retinitis pigmentosa
medicine
mutations in the dynamin family GTPase OPA1 are reportedly the cause of autosomal dominant optic atrophy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xi, Q.; Pauer, G.J.; Ball, S.L.; Rayborn, M.; Hollyfield, J.G.; Peachey, N.S.; Crabb, J.W.; Hagstrom, S.A.
Interaction between the photoreceptor-specific tubby-like protein 1 and the neuronal-specific GTPase dynamin-1
Invest. Ophthalmol. Vis. Sci.
48
2837-2844
2007
Mus musculus
Zhao, L.; Shi, X.; Li, L.; Miller, D.J.
Dynamin 2 associates with complexins and is found in the acrosomal region of mammalian sperm
Mol. Reprod. Dev.
74
750-757
2007
Mus musculus
Misaka, T.; Murate, M.; Fujimoto, K.; Kubo, Y.
The dynamin-related mouse mitochondrial GTPase OPA1 alters the structure of the mitochondrial inner membrane when exogenously introduced into COS-7 cells
Neurosci. Res.
55
123-133
2006
Mus musculus (P58281), Mus musculus
Otsuka, A.; Abe, T.; Watanabe, M.; Yagisawa, H.; Takei, K.; Yamada, H.
Dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells
Biochem. Biophys. Res. Commun.
378
478-482
2009
Mus musculus (P39054)
Otomo, M.; Takahashi, K.; Miyoshi, H.; Osada, K.; Nakashima, H.; Yamaguchi, N.
Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase)
Biol. Pharm. Bull.
31
1489-1495
2008
Mus musculus
Marina-Garcia, N.; Franchi, L.; Kim, Y.G.; Hu, Y.; Smith, D.E.; Boons, G.J.; Nunez, G.
Clathrin- and dynamin-dependent endocytic pathway regulates muramyl dipeptide internalization and NOD2 activation
J. Immunol.
182
4321-4327
2009
Mus musculus
Ferguson, S.M.; De Camilli, P.
Dynamin, a membrane-remodelling GTPase
Nat. Rev. Mol. Cell Biol.
13
75-88
2012
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Belenguer, P.; Pellegrini, L.
The dynamin GTPase OPA1: more than mitochondria?
Biochim. Biophys. Acta
1833
176-183
2013
Homo sapiens (O60313), Mus musculus (P58281)
Takahashi, K.; Otomo, M.; Yamaguchi, N.; Nakashima, H.; Miyoshi, H.
Replacement of Arg-386 with Gly in dynamin 1 middle domain reduced GTPase activity and oligomer stability in the absence of lipids
Biosci. Biotechnol. Biochem.
76
2195-2200
2012
Mus musculus (P39053)
Lomash, R.M.; Gu, X.; Youle, R.J.; Lu, W.; Roche, K.W.
Neurolastin, a dynamin family GTPase, regulates excitatory synapses and spine density
Cell Rep.
12
743-751
2015
Mus musculus
Lomash, R.M.; Petralia, R.S.; Holtzclaw, L.A.; Tsuda, M.C.; Wang, Y.X.; Badger, J.D.; Cameron, H.A.; Youle, R.J.; Roche, K.W.
Neurolastin, a dynamin family GTPase, translocates to mitochondria upon neuronal stress and alters mitochondrial morphology in vivo
J. Biol. Chem.
294
11498-11512
2019
Mus musculus (Q8K1M6)
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