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Validated All-in-One™ qPCR Primer for DNM1L(NM_012062.5) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is a member of the dynamin superfamily of GTPases. Members of the dynamin-related subfamily, including the S. cerevisiae proteins Dnm1 and Vps1, contain the N-terminal tripartite GTPase domain but do not have the pleckstrin homology or proline-rich domains. This protein establishes mitochondrial morphology through a role in distributing mitochondrial tubules throughout the cytoplasm. The gene has 3 alternatively spliced transcripts encoding different isoforms.
Gene References into function
- contributes to mitochondrial division in mammalian cells
- role in peroxisomal fission
- DNM1L performs an essential but transient role in peroxisome division
- This protein mediates scission of the outer mitochondrial membrane, resulting in fragmentation and fission of the mitochondrial network. Inhibition of Drp1 prevented p20-induced fission of mitochondria.
- DLP1 has a role in mitochondrial fission through an interaction with hFis1
- Minimal HdynIV promoter has been characterized and shown that CTCCCAGCA (-108 to -100) sequence may act as a novel transcriptional element for regulating HdynIV gene expression.
- Fis1, Drp1, and Opa1 have roles in apoptosis
- GTPase domain of DLP1 provides an enzymatic function, other domains contain information for assembly and mitochondrial targeting
- Data show that BIK activates recruitment of DRP1 to the surface of the endoplasmic reticulum in intact cells, resulting in mitochondrial fragmentation but little release of cytochrome c to the cytosol.
- Early regulatory GTPase-like function of dynamin precedes late, assembly-dependent steps during which GTP hydrolysis is required for vesicle release.
- Drp1 together with mitochondrial fission protein (hFis1) antogonizes Bcl-2.
- phosphorylation of Drp1 on Ser-585 promotes mitochondrial fission in mitotic cells
- Dnregulation of Drp1 delays but does not inhibit apoptosis, suggesting that mitochondrial fragmentation is not a prerequisite for apoptosis.
- Protein phosphorylation at Ser(637) results in clear alterations in Drp1 function and mitochondrial morphology.
- MARCH5 is required for DRP1-dependent mitochondrial division.
- Results show that Drp1 mediates caspase-independent type III cell death in normal and leukemic cells.
- Precise interactions between a few proteins are required for mitochondrial fusion and division. Among them Drp1, Mfn1, Mfn2 and Opal are considered the most important.
- Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death.
- Drp1 dephosphorylation increases cell vulnerability to apoptosis.
- review of the regulation, activity, and function of dynamin-related protein 1, the main factor for controlled mitochondrial fission [review]
- DLP1 reduction causes mitochondrial abnormalities in sAD fibroblasts, elevated oxidative stress and increased amyloid beta production are likely the potential pathogenic factors that cause DLP1 reduction and abnormal mitochondrial distribution
- CaMKIalpha is a widely expressed protein kinase, suggesting that Ca2+ is likely to be functionally important in the control of mitochondrial dynamics through regulation of Drp1 phosphorylation in neurons and other cell types.
- fragmentation of depolarized mitochondria depends on a loop involving sustained Ca(2+) rise, activation of calcineurin, and dephosphorylation of Drp1 and its translocation to the organelle