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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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antibodies
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stimulate by crosslinking through the C-terminal proline-rich domain of dynamin
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endogenouse rat brain vesicles
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cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
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ionomycin
a calcium ionophore, causes rapid mitochondrial accumulation of actin filaments followed by Drp1 accumulation at the fission site, and increases fission rate
L-phosphatidylserine
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binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
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lipid tubule
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stimulate GTPase activity
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liposome
liposome-stimulated GTPase activity of Dyn1
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Mff protein
mitocjondrial protein Mff alone causes only a slight increase in Drp1 GTPase activity at the concentrations tested, while the combination of Mff and actin filaments causes a substantial increase in Drp1 activity, far beyond the additive effects of either Mff or actin alone
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mitochondrial fission factor
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phosphatidylglycerol
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stimulates
phosphatidylinositol
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stimulates
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
phosphatidylserine
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stimulates
phosphatidylserine liposomes
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phospholipase D
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PLD function as a GTPase activating protein, GAP, through its phox homology domain, PX, which directly activates the GTPase domain of dynamin
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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
actin
actin filaments bind purified Drp1 and increase GTPase activity in a manner that is synergistic with the mitochondrial protein Mff, suggesting a role for direct Drp1/actin interaction
actin
actin filaments increase Drp1's GTPase activity eith a 3.5fold increase. The assembly of filaments of actin is the signal to Drp1 to accumulate on mitochondria and for fission
Arc/Arg3.1
enhances dynamin polymerization and GTPase activity. The activity-regulated cytoskeleton-associated protein, Arc, is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc facilitates the polymerization of Dyn2 and stimulates its GTPase activity under physiologic conditions (37°C and 100 mM NaCl). At lower ionic strength Arc also stabilizes preformed Dyn2 polymers against GTP-dependent disassembly, thereby prolonging assembly-dependent GTP hydrolysis catalyzed by Dyn2. Arc also increases the GTPase activity of Dyn3, an isoform of implicated in dendrite remodeling, but does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214). While residues 195-214 may contribute to dynamin binding, additional binding determinants are likely to be present in the N-terminal portion of Arc. Arc stimulates the assembly-dependent GTPase activity of isozymes Dyn2 and Dyn3. The effect of Arc on GTPase activity of dynamin mirrors its effect on dynamin assembly as measured by turbidity
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Arc/Arg3.1
enhances dynamin polymerization and GTPase activity. The activity-regulated cytoskeleton-associated protein, Arc, is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc increases the GTPase activity of Dyn3, an isoform of implicated in dendrite remodeling. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214). Arc stimulates the assembly-dependent GTPase activity of isozymes Dyn2 and Dyn3. The effect of Arc on GTPase activity of dynamin mirrors its effect on dynamin assembly as measured by turbidity
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cardiolipin
Drp1 binding to anionic lipids such as cardiolipin increases its GTPase activity
cardiolipin
stimulates Drp1, synergistically with mitochondrial fission factor
cardiolipin
stimulates Drp1, synergistically with mitochondrial fission factor
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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Mff-proteoliposome
lipid-stimulated GTPase activity
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Mff-proteoliposome
lipid-stimulated GTPase activity
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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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microtubule
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activates GTPase activity
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microtubules
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activates, binds to carboxyl-terminal proline/arginine-rich domain
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microtubules
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stimulates
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microtubules
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cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
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microtubules
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accelerates GTPase activity up to 150fold, about 4fold activation of ATPase activity
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mitochondrial fission factor
Mff, stimulates Drp1 independently of, but synergistically with cardiolipin
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mitochondrial fission factor
Mff, stimulates Drp1 independently of, but synergistically with cardiolipin
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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
phosphatidylinositol-4,5-bisphosphate
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activates
phosphatidylinositol-4,5-bisphosphate
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binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
Phospholipid
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mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
Phospholipid
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mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
Phospholipid
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stimulates GTPase activity of dynamin
Phospholipid
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acidic phospholipids, cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
Phospholipid
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mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
SH3 domains
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stimulates
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SH3 domains
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stimulation by several recombinant SH3 domains, binding through proline-rich sequence motifs
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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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additional information
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dynamin can self-assemble forming higher order structures such as rings and spirals that exhibit up to 100fold stimulated GTPase activity, conformational changes in the active site accompany self-assembly
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additional information
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robust stimulation of dynamin's GTPase activity upon polymerization
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additional information
interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
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additional information
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robust stimulation of dynamin's GTPase activity upon polymerization
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additional information
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dynamin I and II are stimulated by self-assembly, dynamin II has a greater propensity for self-assembly than neuronal dynamin I
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additional information
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the GAP function of PLD1-PX stimulates the GTPase activity of dynamin by increasing dynamin self-assembly
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additional information
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robust stimulation of dynamin's GTPase activity upon polymerization
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additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
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additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
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additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
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additional information
interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
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additional information
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interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
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