New interfaces on MiD51 for Drp1 recruitment and regulation

PLoS One. 2019 Jan 31;14(1):e0211459. doi: 10.1371/journal.pone.0211459. eCollection 2019.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Dynamins
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism*
  • Guanosine Triphosphate / metabolism*
  • HeLa Cells
  • Humans
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism*
  • Mitochondrial Dynamics*
  • Mitochondrial Proteins / chemistry
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism*
  • Models, Molecular
  • Peptide Elongation Factors / chemistry
  • Peptide Elongation Factors / genetics
  • Peptide Elongation Factors / metabolism*
  • Protein Conformation
  • Sequence Homology

Substances

  • MIEF1 protein, human
  • Microtubule-Associated Proteins
  • Mitochondrial Proteins
  • Peptide Elongation Factors
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • DNM1L protein, human
  • Dynamins

Grants and funding

This project is financially supported by the National 973 Program from the Chinese Ministry of Science and Technology to F.S.(Grants 2014CB910700 and 2011CB910301), and the Strategic Priority Research Program (XDB08030202) to F.S. from the Chinese Academy of Sciences (CAS). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.