Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling
文献类型:期刊论文
作者 | Wang, YG; Du, D; Fang, LH; Yang, G; Zhang, CY; Zeng, R; Ullrich, A; Lottspeich, F; Chen, ZJ |
刊名 | EMBO JOURNAL
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出版日期 | 2006 |
卷号 | 25期号:21页码:5058-5070 |
关键词 | EGFR signaling LIMK2 Par3 phosphotyrosine tight junction |
通讯作者 | Chen, ZJ (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Proteom, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,zjchen@sibs.ac.cn |
英文摘要 | The conserved polarity complex, comprising the partitioning-defective ( Par) proteins Par3 and Par6, and the atypical protein kinase C, functions in various cell-polarization events and asymmetric cell divisions. However, little is known about whether and how external stimuli-induced signals may regulate Par3 function in epithelial cell polarity. Here, we found that Par3 was tyrosine phosphorylated through phosphoproteomic profiling of pervanadate-induced phosphotyrosine proteins. We also demonstrated that the tyrosine phosphorylation event induced by multiple growth factors including epidermal growth factor (EGF) was dependent on activation of Src family kinase (SFK) members c-Src and c-Yes. The tyrosine residue 1127 (Y1127) of Par3 was identified as the major EGF-induced phosphorylation site. Moreover, we found that Y1127 phosphorylation reduced the association of Par3 with LIM kinase 2 (LIMK2), thus enabling LIMK2 to regulate cofilin phosphorylation dynamics. Substitution of Y1127 for phenylalanine impaired the EGF-induced Par3 and LIMK2 dissociation and delayed epithelial tight junction (TJ) assembly considerably. Collectively, these data suggest a novel, phosphotyrosine-dependent fine-tuning mechanism of Par3 in epithelial TJ assembly controlled by the EGF receptor-SFK signaling pathway. |
学科主题 | Biochemistry & Molecular Biology; Cell Biology |
类目[WOS] | Biochemistry & Molecular Biology ; Cell Biology |
关键词[WOS] | GROWTH-FACTOR RECEPTOR ; POLARITY PROTEIN PAR6 ; CANINE KIDNEY-CELLS ; KINASE-C ; ATYPICAL PKC ; MDCK CELLS ; COMPLEX ; ACTIVATION ; SRC ; OCCLUDIN |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000242214900003 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/1797] ![]() |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Wang, YG,Du, D,Fang, LH,et al. Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling[J]. EMBO JOURNAL,2006,25(21):5058-5070. |
APA | Wang, YG.,Du, D.,Fang, LH.,Yang, G.,Zhang, CY.,...&Chen, ZJ.(2006).Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling.EMBO JOURNAL,25(21),5058-5070. |
MLA | Wang, YG,et al."Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling".EMBO JOURNAL 25.21(2006):5058-5070. |
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