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EC Tree
IUBMB Comments An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
The taxonomic range for the selected organisms is: Bos taurus 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,
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dynamin 1
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GTPase activity
Dynamin, testicular
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dynamin-1
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GTPase activity
GTP phosphohydrolase
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guanine triphosphatase
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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phosphatase, guanosine tri-
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GTP + H2O = GDP + phosphate
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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hydrolysis of phosphoric ester
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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.
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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dynamin self-association is not sufficient condition for the expression of maximal GTPase activity, dynamin molecules must be in proper conformation or orientation if they are to form an active oligomer
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GTP + H2O
GDP + phosphate
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highly specific for GTP
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GTP + H2O
GDP + phosphate
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critical step in fission of coated pits to form coated vesicles
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GTP + H2O
GDP + phosphate
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enzyme is essential for budding clathrin-coated vesicles from the plasma membrane
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GTP + H2O
GDP + phosphate
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plays an essential role in synaptic vesicle recycling
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GTP + H2O
GDP + phosphate
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plays an essential role in synaptic vesicle recycling
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GTP + H2O
GDP + phosphate
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involved in clathrin-mediated endocytosis and other vesicular trafficking processes, dynamin has a mechanochemical function in vesicle scission, the GTPase activity of dynamin and the resulting conformation change are essential for endocytosis
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GTP + H2O
GDP + phosphate
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involved in membrane vesiculation
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GTP + H2O
GDP + phosphate
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GTP hydrolysis results in conformational changes in dynamin bound to lipid nanotubes
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GTP + H2O
GDP + phosphate
GTP + H2O
GDP + phosphate
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critical step in fission of coated pits to form coated vesicles
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?
GTP + H2O
GDP + phosphate
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enzyme is essential for budding clathrin-coated vesicles from the plasma membrane
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GTP + H2O
GDP + phosphate
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plays an essential role in synaptic vesicle recycling
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GTP + H2O
GDP + phosphate
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plays an essential role in synaptic vesicle recycling
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GTP + H2O
GDP + phosphate
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involved in clathrin-mediated endocytosis and other vesicular trafficking processes, dynamin has a mechanochemical function in vesicle scission, the GTPase activity of dynamin and the resulting conformation change are essential for endocytosis
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GTP + H2O
GDP + phosphate
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involved in membrane vesiculation
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cyclosporin A
treating BL-3 cells with 0.005 mM cyclosporine depletes mitochondrial dynamin-2
beta,gamma-methyleneguanosine-5'-monophosphate
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guanylyl-iminodiphosphate
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heterotrimeric G protein betagamma subunit complex
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oligomerization of dynamin prevents inhibition
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1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
amphiphysin
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stimulation of dynamin GTPase activity
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anionic liposome
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potent stimulation of dynamin GTPase activity at low ionic strength, activator interacts with the highly basic C-terminal proline/arginine-rich domain of dynamin via ionic interactions that are essentially abrogated at physiologic ionic strength
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Grb2
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activates, binds to carboxyl-terminal proline/arginine-rich domain. Grb2 and phosphatidylinositol 4,5-bisphosphate together increase the dynamin GTPase activity up to 4fold higher than that obtained by these activators tested separately
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microtubule
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potent stimulation of dynamin GTPase activity at low ionic strength, activator interacts with the highly basic C-terminal proline/arginine-rich domain of dynamin via ionic interactions that are essentially abrogated at physiologic ionic strength
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microtubules
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activates, binds to carboxyl-terminal proline/arginine-rich domain
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phosphatidylinositol 3,4-bisphosphate
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weak activation, binds to the pleckstrin homology domain
phosphatidylinositol 4,5-bisphosphate
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activates the GTPase activity of dynamin, specific for D-5 phosphoinositides, activation mechanism, activates also in the presence of 100-130 mM NaCl, the interactions are mediated by the dynamin pleckstrin homology domain
phosphatidylinositol-4,5-bisphosphate
SH3 domain-containing protein
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activates the GTPase activity of dynamin, activation mechanism
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1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
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activates, binds to the pleckstrin homology domain
1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
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activates the GTPase activity of dynamin, specific for D-5 phosphoinositides, activation mechanism, activates also in the presence of 100-130 mM NaCl, the interactions are mediated by the dynamin pleckstrin homology domain
phosphatidylinositol-4,5-bisphosphate
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activates
phosphatidylinositol-4,5-bisphosphate
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best activator, binds to the pleckstrin homology domain. Grb2 and phosphatidylinositol 4,5-bisphosphate together increase the dynamin GTPase activity up to 4fold higher than that obtained by these activators tested separately
additional information
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dynamin is activated by the facilitation of its self-association, GTPase activity is stimulated by any factor that induces the formation of appropriately oriented dynamin polymers, not activated by phosphatidylinositol 4-phosphate or 1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4-diphosphate
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additional information
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oligomerization of dynamin stimulates its GTPase activity
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0.005 - 0.05
GTP
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Km is in the range of 0.005-0.05 mM depending on salt and temperature conditions
0.0067
GTP
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K142A mutant of the GTPase domain of dynamin
0.0076
GTP
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T141Q mutant of the GTPase domain of dynamin
0.0078
GTP
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wild-type dynamin
0.0091
GTP
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T65A mutant of the GTPase domain of dynamin
0.065
GTP
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R66A mutant of the GTPase domain of dynamin
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0.023
GTP
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T65A mutant of the GTPase domain of dynamin
0.083
GTP
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S45N mutant of the GTPase domain of dynamin
0.45
GTP
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R66A mutant of the GTPase domain of dynamin
0.55
GTP
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T141Q mutant of the GTPase domain of dynamin
1.8
GTP
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K142A mutant of the GTPase domain of dynamin
3.1
GTP
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wild-type dynamin
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additional information
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additional information
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assay at room temperature
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UniProt
brenda
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brenda
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brenda
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brenda
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leukotoxin mobilizes dynamin-2 from mitochondria to the cell membrane
brenda
mitochondria are the principal source of dynamin-2 in BL-3 cells
brenda
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brenda
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DYN2_BOVIN
866
0
97836
Swiss-Prot
other Location (Reliability: 3 )
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additional information
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dynamin is characterized by a tetramer/monomer equilibrium. Dynamin molecules must be in proper conformation or orientation if they are to form an active oligomer
additional information
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oligomerization of dynamin stimulates its GTPase activity
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K142A
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mutation in the GTPase domain of dynamin, mutant has a moderately impaired GTPase activity, kinetics
R66A
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mutation in the GTPase domain of dynamin, kinetics
S45N
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mutation in the GTPase domain of dynamin, mutant is defective in GTP binding, kinetics
T141Q
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mutation in the GTPase domain of dynamin, mutant is partially inhibited in its GTPase activity, kinetics
T65A
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mutation in the GTPase domain of dynamin, very low GTPase activity, kinetics
additional information
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point mutants of the GTPase effector domain of dynamin
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wild-type and mutant dynamin is expressed using the baculovirus pBac 4 system, expression in COS-7 cells
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Binns, D.D.; Barylko, B.; Grichine, N.; Atkinson, M.A.L.; Helms, M.K.; Jameson, D.M.; Eccleston, J.F.; Albanesi, J.P.
Correlation between self-association modes and GTPase activation of dynamin
J. Protein Chem.
18
277-290
1999
Bos taurus
brenda
Lin, H.C.; Gilman, A.G.
Regulation of dynamin I GTPase activity by G protein betagamma subunits and phosphatidylinositol 4,5-bisphosphate
J. Biol. Chem.
271
27979-27982
1996
Bos taurus, Homo sapiens
brenda
Shpetner, H.S.; Vallee, R.B.
Dynamin is a GTPase stimulated to high levels of activity by microtubules
Nature
355
733-735
1992
Bos taurus
brenda
Barylko, B.; Binns, D.; Lin, K.M.; Atkinson, M.A.L.; Jameson, D.M.; Yin, H.L.; Albanesi, J.P.
Synergistic activation of dynamin GTPase by Grb2 and phosphoinositides
J. Biol. Chem.
273
3791-3797
1998
Bos taurus
brenda
Barylko, B.; Binns, D.D.; Albanesi, J.P.
Activation of dynamin GTPase activity by phosphoinositides and SH3 domain-containing proteins
Methods Enzymol.
329
486-496
2001
Bos taurus
brenda
Marks, B.; Stowell, M.H.B.; Vallis, Y.; Mills, I.G.; Gibson, A.; Hopkins, C.R.; McMahon, H.T.
GTPase activity of dynamin and resulting conformation change are essential for endocytosis
Nature
410
231-235
2001
Bos taurus
brenda
Yoshida, Y.; Takei, K.
Stimulation of dynamin GTPase activity by amphiphysin
Methods Enzymol.
404
528-537
2005
Bos taurus
brenda
Atapattu, D.N.; Albrecht, R.M.; McClenahan, D.J.; Czuprynski, C.J.
Dynamin-2-dependent targeting of mannheimia haemolytica leukotoxin to mitochondrial cyclophilin D in bovine lymphoblastoid cells
Infect. Immun.
76
5357-5365
2008
Bos taurus (A6H7I5), Bos taurus
brenda