DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, MJ | - |
dc.contributor.author | Sheng, R | - |
dc.contributor.author | Silkov, A | - |
dc.contributor.author | Jung, DJ | - |
dc.contributor.author | Wang, ZG | - |
dc.contributor.author | Xin, Y | - |
dc.contributor.author | Kim, H | - |
dc.contributor.author | Thiagarajan-Rosenkranz, P | - |
dc.contributor.author | Song, S | - |
dc.contributor.author | Yoon, Y | - |
dc.contributor.author | Nam, W | - |
dc.contributor.author | Kim, I | - |
dc.contributor.author | Kim, E | - |
dc.contributor.author | Lee, DG | - |
dc.contributor.author | Chen, Y | - |
dc.contributor.author | Singaram, I | - |
dc.contributor.author | Wang, L | - |
dc.contributor.author | Jang, MH | - |
dc.contributor.author | Hwang, CS | - |
dc.contributor.author | Honig, B | - |
dc.contributor.author | Ryu, S | - |
dc.contributor.author | Lorieau, J | - |
dc.contributor.author | Kim, YM | - |
dc.contributor.author | Cho, W | - |
dc.date.accessioned | 2017-07-19T12:33:36Z | - |
dc.date.available | 2017-07-19T12:33:36Z | - |
dc.date.created | 2016-06-07 | - |
dc.date.issued | 2016-04-07 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/36031 | - |
dc.description.abstract | The Src-homology 2 (SH2) domain is a protein interaction domain that directs myriad phosphotyrosine (pY)-signaling pathways. Genome-wide screening of human SH2 domains reveals that similar to 90% of SH2 domains bind plasma membrane lipids and many have high phosphoinositide specificity. They bind lipids using surface cationic patches separate from pY-binding pockets, thus binding lipids and the pY motif independently. The patches form grooves for specific lipid headgroup recognition or flat surfaces for non-specific membrane binding and both types of interaction are important for cellular function and regulation of SH2 domain-containing proteins. Cellular studies with ZAP70 showed that multiple lipids bind its C-terminal SH2 domain in a spatiotemporally specific manner and thereby exert exquisite spatiotemporal control over its protein binding and signaling activities in T cells. Collectively, this study reveals how lipids control SH2 domain-mediated cellular protein-protein interaction networks and suggest a new strategy for therapeutic modulation of pY-signaling pathways. | - |
dc.language | English | - |
dc.publisher | Cell Press | - |
dc.relation.isPartOf | Molecular Cell | - |
dc.title | SH2 domains serve as lipid binding modules for pTyr-signaling proteins | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/J.MOLCEL.2016.01.027 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Molecular Cell, v.62, no.1, pp.7 - 20 | - |
dc.identifier.wosid | 000374119600004 | - |
dc.date.tcdate | 2019-03-01 | - |
dc.citation.endPage | 20 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 7 | - |
dc.citation.title | Molecular Cell | - |
dc.citation.volume | 62 | - |
dc.contributor.affiliatedAuthor | Hwang, CS | - |
dc.contributor.affiliatedAuthor | Ryu, S | - |
dc.contributor.affiliatedAuthor | Kim, YM | - |
dc.identifier.scopusid | 2-s2.0-84962393747 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 26 | - |
dc.description.scptc | 20 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | TYROSINE KINASE | - |
dc.subject.keywordPlus | PHOSPHOINOSITIDE | - |
dc.subject.keywordPlus | ORGANIZATION | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | RESIDUES | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | DYNAMICS | - |
dc.subject.keywordPlus | ZAP-70 | - |
dc.subject.keywordPlus | GAMMA | - |
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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