MassIVE MSV000084362

Complete Public PXD015534

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

Description

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

Contact

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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