SH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins

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dc.contributor.authorPark, Mi-Jeongko
dc.contributor.authorSheng, Renko
dc.contributor.authorSilkov, Antoninako
dc.contributor.authorJung, Da-Jungko
dc.contributor.authorWang, Zhi-Gangko
dc.contributor.authorXin, Yaoko
dc.contributor.authorKim, Hyunjinko
dc.contributor.authorThiagarajan-Rosenkranz, Pallaviko
dc.contributor.authorSong, Seohyeonko
dc.contributor.authorYoon, Youngdaeko
dc.contributor.authorNam, Wonheeko
dc.contributor.authorKim, Ilshinko
dc.contributor.authorKim, Euiko
dc.contributor.authorLee, Dong-Gyuko
dc.contributor.authorChen, Yongko
dc.contributor.authorSingaram, Indirako
dc.contributor.authorWang, Liko
dc.contributor.authorJang, Myoung Hoko
dc.contributor.authorHwang, Cheol-Sangko
dc.contributor.authorHonig, Barryko
dc.contributor.authorRyu, Sunghoko
dc.contributor.authorLorieau, Justinko
dc.contributor.authorKim, You-Meko
dc.contributor.authorCho, Wonhwako
dc.date.accessioned2018-03-21T02:53:06Z-
dc.date.available2018-03-21T02:53:06Z-
dc.date.created2018-03-14-
dc.date.created2018-03-14-
dc.date.created2018-03-14-
dc.date.issued2016-04-
dc.identifier.citationMOLECULAR CELL, v.62, no.1, pp.7 - 20-
dc.identifier.issn1097-2765-
dc.identifier.urihttp://hdl.handle.net/10203/240764-
dc.description.abstractThe 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.languageEnglish-
dc.publisherCELL PRESS-
dc.titleSH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins-
dc.typeArticle-
dc.identifier.wosid000374119600004-
dc.identifier.scopusid2-s2.0-84962393747-
dc.type.rimsART-
dc.citation.volume62-
dc.citation.issue1-
dc.citation.beginningpage7-
dc.citation.endingpage20-
dc.citation.publicationnameMOLECULAR CELL-
dc.identifier.doi10.1016/j.molcel.2016.01.027-
dc.contributor.localauthorKim, You-Me-
dc.contributor.nonIdAuthorPark, Mi-Jeong-
dc.contributor.nonIdAuthorSheng, Ren-
dc.contributor.nonIdAuthorSilkov, Antonina-
dc.contributor.nonIdAuthorJung, Da-Jung-
dc.contributor.nonIdAuthorWang, Zhi-Gang-
dc.contributor.nonIdAuthorXin, Yao-
dc.contributor.nonIdAuthorKim, Hyunjin-
dc.contributor.nonIdAuthorThiagarajan-Rosenkranz, Pallavi-
dc.contributor.nonIdAuthorSong, Seohyeon-
dc.contributor.nonIdAuthorYoon, Youngdae-
dc.contributor.nonIdAuthorNam, Wonhee-
dc.contributor.nonIdAuthorKim, Ilshin-
dc.contributor.nonIdAuthorKim, Eui-
dc.contributor.nonIdAuthorLee, Dong-Gyu-
dc.contributor.nonIdAuthorChen, Yong-
dc.contributor.nonIdAuthorSingaram, Indira-
dc.contributor.nonIdAuthorWang, Li-
dc.contributor.nonIdAuthorJang, Myoung Ho-
dc.contributor.nonIdAuthorHwang, Cheol-Sang-
dc.contributor.nonIdAuthorHonig, Barry-
dc.contributor.nonIdAuthorRyu, Sungho-
dc.contributor.nonIdAuthorLorieau, Justin-
dc.contributor.nonIdAuthorCho, Wonhwa-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordPlusTYROSINE KINASE-
dc.subject.keywordPlusPLASMA-MEMBRANE-
dc.subject.keywordPlusSCAFFOLD PROTEINS-
dc.subject.keywordPlusLIVING CELLS-
dc.subject.keywordPlusPHOSPHOINOSITIDE-
dc.subject.keywordPlusORGANIZATION-
dc.subject.keywordPlusSPECIFICITY-
dc.subject.keywordPlusRESIDUES-
dc.subject.keywordPlusDYNAMICS-
dc.subject.keywordPlusELECTROSTATICS-
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