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Chinese Academy of Sciences Institutional Repositories Grid
Cation-pi interaction regulates ligand-binding affinity and signaling of integrin alpha(4)beta(7)

文献类型:期刊论文

作者Pan, YP; Zhang, K; Qi, JP; Yue, JA; Springer, TA; Chen, JF
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
出版日期2010
卷号107期号:50页码:21388-21393
通讯作者Springer, TA (reprint author), Harvard Univ, Childrens Hosp, Sch Med, Immune Dis Inst, 3 Blackfan Circle, Boston, MA 02115 USA.,springer@idi.harvard.edu ; jfchen@sibs.ac.cn
英文摘要Integrin alpha(4)beta(7) mediates rolling and firm adhesion of leucocytes, two of the critical steps in leukocyte migration and tissue specific homing. Affinity of alpha(4)beta(7) for ligand is dynamically regulated by three interlinked metal ion-binding sites in beta(7)-subunit I domain. In this study, we found that Phe185 (F185), a highly conserved aromatic residue in beta(7)-subunit, links the specificity-determining loop and the synergistic metal ion-binding site (SyMBS) through cation-pi interaction. Mutations of F185 that disrupted the SyMBS cation-F185 interaction led to deficient firm cell adhesion mediated by high affinity alpha(4)beta(7), and only slightly affected rolling adhesion mediated by low affinity alpha(4)beta(7). Disruption of SyMBS cation-F185 interaction induced partial extension of integrin ectodomain and separation of cytoplasmic tails, and impaired alpha(4)beta(7)-mediated bidirectional signaling. In addition, loss of SyMBS cation-F185 interaction increased paxillin expression and promoted paxillin-integrin binding, leading to deficient cell spreading. Furthermore, integrin alpha(4)beta(7)-mediated cell migration was decreased by the abolishment of SyMBS cation-F185 interaction. Thus, these findings reveal a cation-pi interaction playing vital roles in the regulation of integrin affinity, signaling, and biological functions.
学科主题Science & Technology - Other Topics
类目[WOS]Multidisciplinary Sciences
关键词[WOS]SPECIFICITY-DETERMINING LOOP ; I-LIKE DOMAIN ; CELL-MIGRATION ; BETA-SUBUNIT ; STRUCTURAL BASIS ; CYTOPLASMIC DOMAIN ; CRYSTAL-STRUCTURE ; ALPHA-SUBUNIT ; HYBRID DOMAIN ; ACTIVATION
收录类别SCI
语种英语
WOS记录号WOS:000285521500033
版本出版稿
源URL[http://202.127.25.143/handle/331003/1099]  
专题上海生化细胞研究所_上海生科院生化细胞研究所
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GB/T 7714
Pan, YP,Zhang, K,Qi, JP,et al. Cation-pi interaction regulates ligand-binding affinity and signaling of integrin alpha(4)beta(7)[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2010,107(50):21388-21393.
APA Pan, YP,Zhang, K,Qi, JP,Yue, JA,Springer, TA,&Chen, JF.(2010).Cation-pi interaction regulates ligand-binding affinity and signaling of integrin alpha(4)beta(7).PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,107(50),21388-21393.
MLA Pan, YP,et al."Cation-pi interaction regulates ligand-binding affinity and signaling of integrin alpha(4)beta(7)".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 107.50(2010):21388-21393.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

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