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Proper insertion and topogenesis of membrane proteins in the ER depend on Sec63
DC Field | Value | Language |
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dc.contributor.author | Jung, Sung-jun | - |
dc.contributor.author | Jung, Yunjae | - |
dc.contributor.author | Kim, Hyun Ah | - |
dc.creator | Hyun Ah Kim | - |
dc.date.accessioned | 2020-01-23T07:25:02Z | - |
dc.date.available | 2020-04-05T07:25:02Z | - |
dc.date.created | 2019-09-27 | - |
dc.date.created | 2019-09-27 | - |
dc.date.issued | 2019-09 | - |
dc.identifier.citation | Biochimica et Biophysica Acta - General Subjects, Vol.1863 No.9, pp.1371-1380 | - |
dc.identifier.issn | 0304-4165 | - |
dc.identifier.uri | https://hdl.handle.net/10371/163585 | - |
dc.description.abstract | Background: In eukaryotic cells, biogenesis of proteins destined to the secretory pathway begins from the cytosol. Nascent chains are either co-translationally or post-translationally targeted to the endoplasmic reticulum (ER) and translocated across the membrane through the Sec61 complex. For the post-translational translocation, the Sec62/Sec63 complex is additionally required. Sec63, however, is also shown to mediate co-translational translocation of a subset of proteins, the types and characteristics of proteins that Sec63 mediates in translocation still await to be defined. Methods: To overview the types of proteins that require Sec63 for the ER translocation, we prepared Sec63 mutant lacking the first 39 residues (Sec63_Delta N39) in yeast and assessed initial translocation efficiencies of diverse types of precursors in the sec63_Delta N39 strain by a 5 min metabolic labeling. By employing Blue-Native gel electrophoresis (BN-PAGE), stability of the SEC complex (Sec61 plus Sec62/Sec63 complexes) isolated from cells carrying the Sec63_Delta N39 mutant was examined. Results: Among the various translocation precursors tested, we found that proper sorting of single- and double-pass membrane proteins was severely impaired in addition to post-translational translocation precursor in the sec63_Delta N39 mutant strain. Stability of the SEC complex was compromised upon deletion of the N-terminal 39 residues. Conclusions: The N-terminus of Sec63 is important for stability of the SEC complex and Sec63 is required for proper sorting of membrane proteins in vivo. General significance: Sec63 is essential on insertion of membrane proteins. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | en |
dc.publisher | Elsevier BV | - |
dc.title | Proper insertion and topogenesis of membrane proteins in the ER depend on Sec63 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbagen.2019.06.005 | - |
dc.citation.journaltitle | Biochimica et Biophysica Acta - General Subjects | - |
dc.identifier.wosid | 000480673100006 | - |
dc.identifier.scopusid | 2-s2.0-85067449574 | - |
dc.description.srnd | OAIID:RECH_ACHV_DSTSH_NO:T201906972 | - |
dc.description.srnd | RECH_ACHV_FG:RR00200001 | - |
dc.description.srnd | ADJUST_YN: | - |
dc.description.srnd | EMP_ID:A078040 | - |
dc.description.srnd | CITE_RATE:3.681 | - |
dc.description.srnd | FILENAME:1번 논문_9월예정.pdf | - |
dc.description.srnd | DEPT_NM:생명과학부 | - |
dc.description.srnd | EMAIL:joy@snu.ac.kr | - |
dc.description.srnd | SCOPUS_YN:Y | - |
dc.description.srnd | FILEURL:https://srnd.snu.ac.kr/eXrepEIR/fws/file/7e6af05f-ada8-4f8b-a534-78f995047b85/link | - |
dc.citation.endpage | 1380 | - |
dc.citation.number | 9 | - |
dc.citation.startpage | 1371 | - |
dc.citation.volume | 1863 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Kim, Hyun Ah | - |
dc.identifier.srnd | T201906972 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM MEMBRANE | - |
dc.subject.keywordPlus | SIGNAL-ANCHOR PROTEINS | - |
dc.subject.keywordPlus | ALPHA-FACTOR | - |
dc.subject.keywordPlus | TRANSLOCATION | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | BIP | - |
dc.subject.keywordPlus | POLYPEPTIDE | - |
dc.subject.keywordPlus | TRANSPORT | - |
dc.subject.keywordAuthor | Endoplasmic reticulum (ER) | - |
dc.subject.keywordAuthor | Protein translocation | - |
dc.subject.keywordAuthor | Protein targeting | - |
dc.subject.keywordAuthor | Sec63 | - |
dc.subject.keywordAuthor | Sec62 | - |
dc.subject.keywordAuthor | Sec61 | - |
dc.subject.keywordAuthor | Signal sequence | - |
dc.subject.keywordAuthor | Saccharomyces cerevisiae | - |
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