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Literature summary extracted from

  • Ferguson, S.M.; De Camilli, P.
    Dynamin, a membrane-remodelling GTPase (2012), Nat. Rev. Mol. Cell Biol., 13, 75-88.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.5.5 additional information robust stimulation of dynamin's GTPase activity upon polymerization Mus musculus
3.6.5.5 additional information robust stimulation of dynamin's GTPase activity upon polymerization Homo sapiens
3.6.5.5 additional information robust stimulation of dynamin's GTPase activity upon polymerization Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.5.5 clathrin-coated vesicle dynamin is a general component of clathrin-coated endocytic pits Drosophila melanogaster 30136
-
3.6.5.5 clathrin-coated vesicle dynamin is a general component of clathrin-coated endocytic pits Mus musculus 30136
-
3.6.5.5 clathrin-coated vesicle dynamin is a general component of clathrin-coated endocytic pits Homo sapiens 30136
-
3.6.5.5 clathrin-coated vesicle dynamin is a general component of clathrin-coated endocytic pits Rattus norvegicus 30136
-
3.6.5.5 clathrin-coated vesicle dynamin is a general component of clathrin-coated endocytic pits Caenorhabditis elegans 30136
-
3.6.5.5 mitochondrial membrane dynamin-related protein 1, DRP1 Homo sapiens 31966
-
3.6.5.5 peroxisome dynamin-related protein 1, DRP1 Homo sapiens 5777
-
3.6.5.5 plasma membrane
-
 Drosophila melanogaster 5886
-
3.6.5.5 plasma membrane
-
 Mus musculus 5886
-
3.6.5.5 plasma membrane
-
 Homo sapiens 5886
-
3.6.5.5 plasma membrane
-
 Rattus norvegicus 5886
-
3.6.5.5 plasma membrane
-
 Caenorhabditis elegans 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.5 additional information Homo sapiens 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 ?
-
 ?
3.6.5.5 additional information Mus musculus 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 ?
-
 ?
3.6.5.5 additional information Rattus norvegicus 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.5 Caenorhabditis elegans
-
 single gene
-
3.6.5.5 Drosophila melanogaster
-
 single gene
-
3.6.5.5 Homo sapiens
-
 three dynamin isoforms, dynamin1-dynamin3, and multiple splice variants for each of the three dynamins
-
3.6.5.5 Mus musculus
-
 three dynamin isoforms, dynamin1-dynamin3, and multiple splice variants for each of the three dynamins
-
3.6.5.5 Rattus norvegicus
-
 three dynamin isoforms, dynamin1-dynamin3, and multiple splice variants for each of the three dynamins
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.5.5 brain isozymes dymain 1, dymanin 2, and dynamin 3 Mus musculus
-
3.6.5.5 brain isozymes dymain 1, dymanin 2, and dynamin 3 Homo sapiens
-
3.6.5.5 brain isozymes dymain 1, dymanin 2, and dynamin 3 Rattus norvegicus
-
3.6.5.5 lung isozymes dymanin 2 and dynamin 3 Mus musculus
-
3.6.5.5 lung isozymes dymanin 2 and dynamin 3 Homo sapiens
-
3.6.5.5 lung isozymes dymanin 2 and dynamin 3 Rattus norvegicus
-
3.6.5.5 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 Mus musculus
-
3.6.5.5 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 Homo sapiens
-
3.6.5.5 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 Rattus norvegicus
-
3.6.5.5 neuron isozyme dynamin2, isozyme dynamin 1 is selectively expressed at high levels in neurons and is generally not present in non-neuronal tissues Rattus norvegicus
-
3.6.5.5 neuron isozyme dynamin2, isozyme dynamin 1 is selectively expressed at high levels in neurons and is gen­erally not present in non-neuronal tissues Mus musculus
-
3.6.5.5 neuron isozyme dynamin2, isozyme dynamin 1 is selectively expressed at high levels in neurons and is gen­erally not present in non-neuronal tissues Homo sapiens
-
3.6.5.5 testis isozymes dymanin 2 and dynamin 3 Mus musculus
-
3.6.5.5 testis isozymes dymanin 2 and dynamin 3 Homo sapiens
-
3.6.5.5 testis isozymes dymanin 2 and dynamin 3 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.5 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 Homo sapiens ?
-
 ?
3.6.5.5 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 Mus musculus ?
-
 ?
3.6.5.5 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 Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.5.5 More structure-function relationship, 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 Drosophila melanogaster
3.6.5.5 More structure-function relationship, 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 Caenorhabditis elegans
3.6.5.5 More 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 Mus musculus
3.6.5.5 More 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 Homo sapiens
3.6.5.5 More 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 Rattus norvegicus
3.6.5.5 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 Drosophila melanogaster
3.6.5.5 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 Caenorhabditis elegans
3.6.5.5 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 Mus musculus
3.6.5.5 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 Homo sapiens
3.6.5.5 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 Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
3.6.5.5 dynamin
-
 Drosophila melanogaster
3.6.5.5 dynamin
-
 Mus musculus
3.6.5.5 dynamin
-
 Homo sapiens
3.6.5.5 dynamin
-
 Rattus norvegicus
3.6.5.5 dynamin
-
 Caenorhabditis elegans
3.6.5.5 GTPase dynamin
-
 Drosophila melanogaster
3.6.5.5 GTPase dynamin
-
 Mus musculus
3.6.5.5 GTPase dynamin
-
 Homo sapiens
3.6.5.5 GTPase dynamin
-
 Rattus norvegicus
3.6.5.5 GTPase dynamin
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
3.6.5.5 malfunction dynamin gene muta­tions are responsible for the temperature-sensitive paralytic phenotype of Drosophila melanogaster shibire mutants. The mutants show paralysis resulting from the neuronal activity-dependent depletion of synaptic vesicles, which is accompanied by the accumulation of arrested collared endocytic pits at the presynaptic plasma membrane Drosophila melanogaster
3.6.5.5 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 Mus musculus
3.6.5.5 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 Rattus norvegicus
3.6.5.5 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. Multiple unique missense mutations, or short deletions, within the middle, PH and stalk domains of dynamin 2 in patients with two autosomal-dominant genetic con­ditions are involved in the Charcot-Marie-Tooth disease and centronuclear myopathy, while dynamin 1 might be involved in epilepsy Homo sapiens
3.6.5.5 metabolism GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell Rattus norvegicus
3.6.5.5 metabolism GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events through­out the cell Drosophila melanogaster
3.6.5.5 metabolism GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events through­out the cell Mus musculus
3.6.5.5 metabolism GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events through­out the cell Homo sapiens
3.6.5.5 metabolism GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events through­out the cell Caenorhabditis elegans
3.6.5.5 additional information structure-function relationship, overview. 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 Drosophila melanogaster
3.6.5.5 additional information structure-function relationship, overview. 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 Caenorhabditis elegans
3.6.5.5 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 Mus musculus
3.6.5.5 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 Homo sapiens
3.6.5.5 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 Rattus norvegicus
3.6.5.5 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 Mus musculus
3.6.5.5 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 interacts both directly and indirectly with the cytoskeleton, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis Rattus norvegicus
3.6.5.5 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. Dynamin interacts both directly and indirectly with the cytoskeleton, overview Drosophila melanogaster
3.6.5.5 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. Dynamin interacts both directly and indirectly with the cytoskeleton, overview Caenorhabditis elegans
3.6.5.5 physiological function dynamin drives membrane fission, mechanism, overview. Dynamin-related protein 1, DRP1, is important for the fission of mitochondria and peroxisomes. 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 interacts both directly and indirectly with the cytoskeleton, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamins 1 and 3 play an important part in the endocytosis of neurotransmitter receptors, overview. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis Homo sapiens