| Post Translational Modifications | Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-616 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission. Phosphorylated in a circadian manner at Ser-637. Dephosphorylated by PGAM5. Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity. S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. Ubiquitination by MARCHF5 affects mitochondrial morphology. O-GlcNAcylation augments the level of the GTP-bound active form of DNM1L and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-637. |
| Function | Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane. Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis.this requirement may depend upon the cell type and the physiological apoptotic cues. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles.the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production. Isoform 1: Inhibits peroxisomal division when overexpressed. Isoform 4: Inhibits peroxisomal division when overexpressed. |
| Protein Name | Dynamin-1-Like ProteinDnm1p/Vps1p-Like ProteinDvlpDynamin Family Member Proline-Rich Carboxyl-Terminal Domain LessDympleDynamin-Like ProteinDynamin-Like Protein 4Dynamin-Like Protein IvHdynivDynamin-Related Protein 1 |
| Database Links | Reactome: R-HSA-75153 |
| Cellular Localisation | CytoplasmCytosolGolgi ApparatusEndomembrane SystemPeripheral Membrane ProteinMitochondrion Outer MembranePeroxisomeMembraneClathrin-Coated PitCytoplasmic VesicleSecretory VesicleSynaptic Vesicle MembraneMainly CytosolicRecruited By Rala And Ralbp1 To Mitochondrion During MitosisTranslocated To The Mitochondrial Membrane Through O-Glcnacylation And Interaction With Fis1Colocalized With Marchf5 At Mitochondrial MembraneLocalizes To Mitochondria At Sites Of DivisionLocalizes To Mitochondria Following Necrosis InductionRecruited To The Mitochondrial Outer Membrane By Interaction With Mief1Mitochondrial Recruitment Is Inhibited By C11orf65/MfiAssociated With Peroxisomal MembranesPartly Recruited There By Pex11bMay Also Be Associated With Endoplasmic Reticulum Tubules And Cytoplasmic Vesicles And Found To Be PerinuclearIn Some Cell TypesLocalizes To The Golgi ComplexBinds To Phospholipid Membranes |
| Alternative Protein Names | Dynamin-1-Like Protein proteinDnm1p/Vps1p-Like Protein proteinDvlp proteinDynamin Family Member Proline-Rich Carboxyl-Terminal Domain Less proteinDymple proteinDynamin-Like Protein proteinDynamin-Like Protein 4 proteinDynamin-Like Protein Iv proteinHdyniv proteinDynamin-Related Protein 1 proteinDNM1L proteinDLP1 proteinDRP1 protein |
Information sourced from Uniprot.org
