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Activation of DRP1 by cellular kinase triggers its translocation to mitochondria through its interaction with mitochondrial outer membrane proteins such as mitochondrial fission protein-1, mitochondrial fission factor, and mitochondrial elongation factor-1 and -22.
The specificity or affinity of Drp1 to bind the adaptor fission proteins and OMM receptors to fragment the mitochondrial network is mainly regulated by Drp1 cellular distribution, the oligomer pool, the presence of Drp1 isoforms, PTMs and GTPase activity.
This suggests that DRP1 is likely to play at least two roles in the apoptotic response in pluripotent cells. First, it reduces the effect of the pro-apoptotic roles of BCL-2 family members, and second, it promotes cytochrome c release by helping the remodeling of the mitochondrial cristae.
In cells, Drp1 is regulated by several factors including Drp1 receptors, actin filaments, cardiolipin, and phosphorylation at two sites: S579 and S600. Commonly, phosphorylation of S579 is considered activating, while S600 phosphorylation is considered inhibiting.
Cdk1 kinase requires an activating partnera cyclin. Cyclin B is a pivotal activator of Cdk1 in mitosis. During mitotic exit, cyclin B is degraded by the ubiquitin-proteasome pathway (Glotzer et al., 1991).
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Dynamin-1-like protein is a GTPase that regulates mitochondrial fission. In humans, dynamin-1-like protein, which is typically referred to as dynamin-related protein 1 (Drp1), is encoded by the DNM1L gene and is part of the dynamin superfamily (DSP) family of proteins.
Hypoxia results in the activation of heterodimeric HIF-1, enabling it to bind to cis elements of responsive genes. HIF-1 interacts specifically with p300/CBP, a transcriptional co-activator, thereby up-regulating gene expression (15). Our studies address the mechanism responsible for HIF-1 activation by hypoxia.

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