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DC Field | Value | Language |
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dc.citation.endPage | 12120 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 12109 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 117 | - |
dc.contributor.author | Kwak, Chulhwan | - |
dc.contributor.author | Shin Sanghee | - |
dc.contributor.author | Park, Jong-Seok | - |
dc.contributor.author | Jung, Minkyo | - |
dc.contributor.author | Njung, 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 | 2023-12-21T17:36:49Z | - |
dc.date.available | 2023-12-21T17:36:49Z | - |
dc.date.created | 2020-05-16 | - |
dc.date.issued | 2020-06 | - |
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.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.117, no.22, pp.12109 - 12120 | - |
dc.identifier.doi | 10.1073/pnas.1916584117 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-85085905292 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/32148 | - |
dc.identifier.url | https://www.pnas.org/content/early/2020/05/14/1916584117 | - |
dc.identifier.wosid | 000538147800039 | - |
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.description.isOpenAccess | FALSE | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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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