Num1 anchors mitochondria to the plasma membrane via two domains with different lipid binding specificities

Holly A. Ping, Lauren M. Kraft, Wei Ting Chen, Amy E. Nilles, Laura L. Lackner*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

The mitochondria-ER cortex anchor (MECA) is required for proper mitochondrial distribution and functions by tethering mitochondria to the plasma membrane. The core component of MECA is the multidomain protein Num1, which assembles into clusters at the cell cortex. We show Num1 adopts an extended, polarized conformation. Its N-terminal coiled-coil domain (Num1CC) is proximal to mitochondria, and the C-terminal pleckstrin homology domain is associated with the plasma membrane. We find that Num1CC interacts directly with phospholipid membranes and displays a strong preference for the mitochondria-specific phospholipid cardiolipin. This direct membrane interaction is critical for MECA function. Thus, mitochondrial anchoring is mediated by a protein that interacts directly with two different membranes through lipid-specific binding domains, suggesting a general mechanism for interorganelle tethering.

Original languageEnglish (US)
Pages (from-to)513-524
Number of pages12
JournalJournal of Cell Biology
Volume213
Issue number5
DOIs
StatePublished - 2016

ASJC Scopus subject areas

  • Cell Biology

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