Contact-ID, a tool for profiling organelle contact sites, reveals regulatory proteins of mitochondrial associated membrane formation

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Title
Contact-ID, a tool for profiling organelle contact sites, reveals regulatory proteins of mitochondrial associated membrane formation
Author
Kwak, ChulhwanShin SangheePark, Jong-SeokJung, MinkyoNjung, Truong Thi MyKang, Myeong-GyunLee, ChaiheonKwon, Tae-HyukPark, Sang KiMun, Ji YoungKim, Jong-SeoRhee, Hyun-Woo
Issue Date
2020-05
Publisher
National Academy of Sciences
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Abstract
The mitochondria-associated membrane (MAM) has emerged as a cellular signaling hub regulating various cellular processes. However, its molecular components remain unclear owing to lack of reliable methods to purify the intact MAM proteome in a physiological context. Here, we introduce Contact-ID, a split-pair system of BioID with strong activity, for identification of the MAM proteome in live cells. Contact-ID specifically labeled proteins proximal to the contact sites of the endoplasmic reticulum (ER) and mitochondria, and thereby identified 115 MAM-specific proteins. The identified MAM proteins were largely annotated with the outer mitochondrial membrane (OMM) and ER membrane proteins with MAM-related functions: e.g., FKBP8, an OMM protein, facilitated MAM formation and local calcium transport at the MAM. Furthermore, the definitive identification of biotinylation sites revealed membrane topologies of 85 integral membrane proteins. Contact-ID revealed regulatory proteins for MAM formation and could be reliably utilized to profile the proteome at any organelle–membrane contact sites in live cells.
URI
https://scholarworks.unist.ac.kr/handle/201301/32148
URL
https://www.pnas.org/content/early/2020/05/14/1916584117
DOI
10.1073/pnas.1916584117
ISSN
0027-8424
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SNS_Journal Papers
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