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J Cell Biol. 2017 Oct 2;216(10):3219-3229. doi: 10.1083/jcb.201610055. Epub 2017 Sep 1.

Vps13-Mcp1 interact at vacuole-mitochondria interfaces and bypass ER-mitochondria contact sites.

Author information

1
ETH Zürich, Institute of Biochemistry, Zürich, Switzerland.
2
Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
3
ETH Zürich, Institute of Biochemistry, Zürich, Switzerland benoit.kornmann@bc.biol.ethz.ch.

Abstract

Membrane contact sites between endoplasmic reticulum (ER) and mitochondria, mediated by the ER-mitochondria encounter structure (ERMES) complex, are critical for mitochondrial homeostasis and cell growth. Defects in ERMES can, however, be bypassed by point mutations in the endosomal protein Vps13 or by overexpression of the mitochondrial protein Mcp1. How this bypass operates remains unclear. Here we show that the mitochondrial outer membrane protein Mcp1 functions in the same pathway as Vps13 by recruiting it to mitochondria and promoting its association to vacuole-mitochondria contacts. Our findings support a model in which Mcp1 and Vps13 work as functional effectors of vacuole-mitochondria contact sites, while tethering is mediated by other factors, including Vps39. Tethered and functionally active vacuole-mitochondria interfaces then compensate for the loss of ERMES-mediated ER-mitochondria contact sites.

PMID:
28864540
PMCID:
PMC5626531
DOI:
10.1083/jcb.201610055
[Indexed for MEDLINE]
Free PMC Article

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