Abstract
Mitochondria form intricate networks through fission and fusion events. Here, we identify mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) anchored in the mitochondrial outer membrane. MiD49/51 form foci and rings around mitochondria similar to the fission mediator dynamin-related protein 1 (Drp1). MiD49/51 directly recruit Drp1 to the mitochondrial surface, whereas their knockdown reduces Drp1 association, leading to unopposed fusion. Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin. Thus, MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondria.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Actins / metabolism
-
Amino Acid Sequence
-
Animals
-
COS Cells
-
Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
-
Cell Line
-
Chlorocebus aethiops
-
HeLa Cells
-
Humans
-
Membrane Potential, Mitochondrial / drug effects
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism*
-
Mice
-
Microtubule-Associated Proteins / metabolism
-
Mitochondria / metabolism*
-
Mitochondria / pathology
-
Mitochondrial Membranes / metabolism*
-
Mitochondrial Proteins / genetics
-
Mitochondrial Proteins / metabolism*
-
Molecular Sequence Data
-
Peptide Elongation Factors / genetics
-
Peptide Elongation Factors / metabolism*
-
Protein Transport / genetics
-
RNA Interference
-
Receptors, Cytoplasmic and Nuclear / genetics
-
Receptors, Cytoplasmic and Nuclear / metabolism*
-
Sequence Alignment
-
Uncoupling Agents / pharmacology
Substances
-
Actins
-
MIEF1 protein, human
-
MIEF2 protein, mouse
-
Membrane Proteins
-
MiD51 protein, mouse
-
Microtubule-Associated Proteins
-
Mitochondrial Proteins
-
Peptide Elongation Factors
-
Receptors, Cytoplasmic and Nuclear
-
Uncoupling Agents
-
Carbonyl Cyanide m-Chlorophenyl Hydrazone