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 MAMformation and could be reliably utilized to profile the proteome at any organelle–membrane contact sites in live cells.
[doi:10.25345/C5FD3T]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: MAM ; Contact-ID ; membrane contact sites
Principal Investigators: (in alphabetical order) |
Hyun-Woo Rhee, Seoul National University, Korea Ji Young Mun, Korea Brain Research Institute, Korea Jong-Seo Kim, Seoul National University, Korea Sang Ki Park, Pohang University of Science and Technology, Korea |
Submitting User: | sunnyshin54 |
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