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Contact-ID, a tool for profiling organelle contact sites, reveals regulatory proteins of mitochondrial-associated membrane formation
DC Field | Value | Language |
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dc.contributor.author | Kwak, Chulhwan | - |
dc.contributor.author | Shin, Sanghee | - |
dc.contributor.author | Park, Jong-Seok | - |
dc.contributor.author | Jung, Minkyo | - |
dc.contributor.author | Nhung, Truong Thi My | - |
dc.contributor.author | Kang, Myeong-Gyun | - |
dc.contributor.author | Lee, Chaiheon | - |
dc.contributor.author | Kwon, Tae-Hyuk | - |
dc.contributor.author | Park, Sang Ki | - |
dc.contributor.author | Mun, Ji Young | - |
dc.contributor.author | Kim, Jong-Seo | - |
dc.contributor.author | Rhee, Hyun-Woo | - |
dc.date.accessioned | 2024-05-14T06:48:18Z | - |
dc.date.available | 2024-05-14T06:48:18Z | - |
dc.date.created | 2020-06-29 | - |
dc.date.issued | 2020-06 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America, Vol.117 No.22, pp.12109-12120 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://hdl.handle.net/10371/201883 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.publisher | National Academy of Sciences | - |
dc.title | Contact-ID, a tool for profiling organelle contact sites, reveals regulatory proteins of mitochondrial-associated membrane formation | - |
dc.type | Article | - |
dc.identifier.doi | 10.1073/pnas.1916584117 | - |
dc.citation.journaltitle | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.identifier.wosid | 000538147800039 | - |
dc.identifier.scopusid | 2-s2.0-85085905292 | - |
dc.citation.endpage | 12120 | - |
dc.citation.number | 22 | - |
dc.citation.startpage | 12109 | - |
dc.citation.volume | 117 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Kim, Jong-Seo | - |
dc.contributor.affiliatedAuthor | Rhee, Hyun-Woo | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM | - |
dc.subject.keywordPlus | ASCORBATE PEROXIDASE | - |
dc.subject.keywordPlus | PROTEOMIC ANALYSIS | - |
dc.subject.keywordPlus | ER MEMBRANES | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | AVAILABILITY | - |
dc.subject.keywordPlus | ARCHITECTURE | - |
dc.subject.keywordPlus | METABOLISM | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | STRESS | - |
dc.subject.keywordAuthor | mitochondria-associated membrane (MAM) | - |
dc.subject.keywordAuthor | membrane contact site | - |
dc.subject.keywordAuthor | proximity labeling | - |
dc.subject.keywordAuthor | membrane protein topology | - |
dc.subject.keywordAuthor | FKBP8 | - |
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