Open AccessNew interfaces on MiD51 for Drp1 recruitment and regulation
Author(s) -
Jun Ma,
Yujia Zhai,
Ming Chen,
Kai Zhang,
Quan Chen,
Xiaoyun Pang,
Fei Sun
Publication year - 2019
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0211459
Subject(s) - mitochondrial fission , mechanism (biology) , microbiology and biotechnology , dynamin , biology , mitochondrion , dnm1l , gtp' , receptor , biophysics , physics , genetics , biochemistry , endocytosis , quantum mechanics , enzyme
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.