Recombinant Human DRP1 protein (GST tag N-Terminus)
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(2 Publications)
Recombinant Human DRP1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 710 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
DLP1, DRP1, DNM1L, Dynamin-1-like protein, Dnm1p/Vps1p-like protein, Dynamin family member proline-rich carboxyl-terminal domain less, Dynamin-like protein, Dynamin-like protein 4, Dynamin-like protein IV, Dynamin-related protein 1, DVLP, Dymple, HdynIV
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human DRP1 protein (GST tag N-Terminus) (AB153041)
ab153041 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
DRP1 regulates mitochondrial morphology by controlling mitochondrial division. This process is essential in maintaining the balance between mitochondrial fission and fusion which affects mitochondrial distribution and function. DRP1 also associates with protein complexes involved in this dynamic balance including MFF (mitochondrial fission factor) and FIS1 (fission 1 protein). Phosphorylation state of DRP1 influences its activity; different phosphorylation sites either activate or inhibit its function.
Pathways
The mechanical action of DRP1 integrates closely into the mitochondrial quality control and apoptosis pathways. Mitochondrial fission driven by DRP1 is necessary for the removal of damaged mitochondria through mitophagy. It also influences the apoptotic pathway where DRP1 translocates to mitochondria under pro-apoptotic signals often in interaction with proteins such as Bax and Bak that promote cytochrome c release. This relationship affects cell survival and energy homeostasis.
Specifications
Form
Liquid
General info
Function
Functions in mitochondrial and peroxisomal division (PubMed : 11514614, PubMed : 12499366, PubMed : 17301055, PubMed : 17460227, PubMed : 17553808, PubMed : 18695047, PubMed : 18838687, PubMed : 19342591, PubMed : 19411255, PubMed : 19638400, PubMed : 23283981, PubMed : 23530241, PubMed : 23921378, PubMed : 26992161, PubMed : 27145208, PubMed : 27145933, PubMed : 27301544, PubMed : 27328748, PubMed : 29478834, PubMed : 32439975, PubMed : 32484300, PubMed : 9570752, PubMed : 9786947). 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 (PubMed : 23530241, PubMed : 23584531, PubMed : 33850055). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed : 23283981, PubMed : 23921378, PubMed : 29899447). 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 (PubMed : 29899447). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed : 32484300). Plays an important role in mitochondrial fission during mitosis (PubMed : 19411255, PubMed : 26992161, PubMed : 27301544, PubMed : 27328748). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (PubMed : 17460227, PubMed : 26992161, PubMed : 27145208, PubMed : 27301544, PubMed : 27328748). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). 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 (By similarity). Required for formation of endocytic vesicles (PubMed : 20688057, PubMed : 23792689, PubMed : 9570752). 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 (PubMed : 17015472, PubMed : 23792689). Required for programmed necrosis execution (PubMed : 22265414). Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production (PubMed : 29478834).. Isoform 1. Inhibits peroxisomal division when overexpressed.. Isoform 4. Inhibits peroxisomal division when overexpressed.
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Post-translational modifications
Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (PubMed:17301055, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:23283981, PubMed:29478834, PubMed:33850055). Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (PubMed:17553808, PubMed:18695047, PubMed:23283981, PubMed:29478834). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (PubMed:18838687). Phosphorylation on Ser-616 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission (PubMed:18838687, PubMed:21822277, PubMed:32484300). Phosphorylated in a circadian manner at Ser-637 (PubMed:29478834). Dephosphorylated by PGAM5 (PubMed:32439975).. 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 (By similarity).
Target data
Publications (2)
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British journal of pharmacology 176:4574-4591 PubMed31389613
2019
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Free radical biology & medicine 143:70-83 PubMed31377418
2019
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