DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, GH | - |
dc.contributor.author | Ahn, T | - |
dc.contributor.author | Kim, DS | - |
dc.contributor.author | Park, SJ | - |
dc.contributor.author | Lee, YC | - |
dc.contributor.author | Yoo, WH | - |
dc.contributor.author | Jung, SJ | - |
dc.contributor.author | Yang, JS | - |
dc.contributor.author | Kim, S | - |
dc.contributor.author | Muhlrad, A | - |
dc.contributor.author | Seo, YR | - |
dc.contributor.author | Chae, SW | - |
dc.contributor.author | Kim, HR | - |
dc.contributor.author | Chae, HJ | - |
dc.date.accessioned | 2015-06-25T02:49:20Z | - |
dc.date.available | 2015-06-25T02:49:20Z | - |
dc.date.created | 2010-04-13 | - |
dc.date.issued | 2010-04-01 | - |
dc.identifier.issn | 0270-7306 | - |
dc.identifier.other | 2015-OAK-0000020427 | en_US |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/11697 | - |
dc.description.abstract | Bax inhibitor 1 (BI-1), a transmembrane protein with Ca2+ channel-like activity, has antiapoptotic and anticancer activities. Cells overexpressing BI-1 demonstrated increased cell adhesion. Using a proteomics tool, we found that BI-1 interacted with gamma-actin via leucines 221 and 225 and could control actin polymerization and cell adhesion. Among BI-1(-/-) cells and cells transfected with BI-1 small interfering RNA (siRNA), levels of actin polymerization and cell adhesion were lower than those among BI-1(+/+) cells and cells transfected with nonspecific siRNA. BI-1 acts as a leaky Ca2+ channel, but mutations of the actin binding sites (L221A, L225A, and L221A/L225A) did not change intra-endoplasmic reticulum Ca2+, although deleting the C-terminal motif (EKDKKKEKK) did. However, store-operated Ca2+ entry (SOCE) is activated in cells expressing BI-1 but not in cells expressing actin binding site mutants, even those with the intact C-terminal motif. Consistently, actin polymerization and cell adhesion were inhibited among all the mutant cells. Compared to BI-1(+/+) cells, BI-1(-/-) cells inhibited SOCE, actin polymerization, and cell adhesion. Endogenous BI-1 knockdown cells showed a similar pattern. The C-terminal peptide of BI-1 (LMMLILAMNRKDKKKEKK) polymerized actin even after the deletion of four or six charged C-terminal residues. This indicates that the actin binding site containing L221 to D231 of BI-1 is responsible for actin interaction and that the C-terminal motif has only a supporting role. The intact C-terminal peptide also bundled actin and increased cell adhesion. The results of experiments with whole recombinant BI-1 reconstituted in membranes also coincide well with the results obtained with peptides. In summary, BI-1 increased actin polymerization and cell adhesion through Ca2+ regulation and actin interaction. | - |
dc.description.statementofresponsibility | open | en_US |
dc.language | English | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.relation.isPartOf | MOLECULAR AND CELLULAR BIOLOGY | - |
dc.rights | BY_NC_ND | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/kr | en_US |
dc.title | Bax Inhibitor 1 Increases Cell Adhesion through Actin Polymerization: Involvement of Calcium and Actin Binding | - |
dc.type | Article | - |
dc.contributor.college | 정보전자융합공학부 | en_US |
dc.identifier.doi | 10.1128/MCB.01357-09 | - |
dc.author.google | Lee, Geum-Hwa | en_US |
dc.author.google | Ahn, Taeho | en_US |
dc.author.google | Chae, | en_US |
dc.author.google | Kim, Hyung-Ryong | en_US |
dc.author.google | Chae, Soo-Wan | en_US |
dc.author.google | Seo, Young-Rok | en_US |
dc.author.google | Muhlrad, Andras | en_US |
dc.author.google | Kim, Sanguk | en_US |
dc.author.google | Yang, Jae-Seong | en_US |
dc.author.google | Jung, Sung Jun | en_US |
dc.author.google | Yoo, Wan Hee | en_US |
dc.author.google | Lee, Yong Chul | en_US |
dc.author.google | Park, Seoung Ju | en_US |
dc.author.google | Kim, Do-Sung | en_US |
dc.relation.volume | 30 | en_US |
dc.relation.issue | 7 | en_US |
dc.relation.startpage | 1800 | en_US |
dc.relation.lastpage | 1813 | en_US |
dc.contributor.id | 10136479 | en_US |
dc.relation.journal | MOLECULAR AND CELLULAR BIOLOGY | en_US |
dc.relation.index | SCI급, SCOPUS 등재논문 | en_US |
dc.relation.sci | SCI | en_US |
dc.collections.name | Journal Papers | en_US |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | MOLECULAR AND CELLULAR BIOLOGY, v.30, no.7, pp.1800 - 1813 | - |
dc.identifier.wosid | 000275302000018 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 1813 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 1800 | - |
dc.citation.title | MOLECULAR AND CELLULAR BIOLOGY | - |
dc.citation.volume | 30 | - |
dc.contributor.affiliatedAuthor | Kim, S | - |
dc.identifier.scopusid | 2-s2.0-77949355135 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 18 | - |
dc.description.scptc | 19 | * |
dc.date.scptcdate | 2018-10-274 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | PANCREATIC BETA-CELLS | - |
dc.subject.keywordPlus | CDNA MICROARRAY ANALYSIS | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM | - |
dc.subject.keywordPlus | CA2+ | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | MIGRATION | - |
dc.subject.keywordPlus | CHANNEL | - |
dc.subject.keywordPlus | CANCER | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | PREDICTION | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
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