New interfaces on MiD51 for Drp1 recruitment and regulation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30703167.
- Also identified by DOI 10.1371/journal.pone.0211459 and PMC identifier 6355003.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Mitochondrial fission is facilitated by dynamin-related protein Drp1 and a variety of its receptors. However, the molecular mechanism of how Drp1 is recruited to the mitochondrial surface by receptors MiD49 and MiD51 remains elusive. Here, we showed that the interaction between Drp1 and MiD51 is regulated by GTP binding and depends on the polymerization of Drp1. We identified two regions on MiD51 that directly bind to Drp1, and found that dimerization of MiD51, relevant to residue C452, is required for mitochondrial dynamics regulation. Our Results have suggested a multi-faceted regulatory mechanism for the interaction between Drp1 and MiD51 that illustrates the potentially complicated and tight regulation of mitochondrial fission.
Medical subject headings
- GTP Phosphohydrolases
- Guanosine Triphosphate
- Microtubule-Associated Proteins
- Mitochondrial Dynamics
- Mitochondrial Proteins
- Peptide Elongation Factors