Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST

Te Jung Lu, Wen Yang Lai, Chi Ying F Huang, Wan Jung Hsieh, Jau Song Yu, Ya Ju Hsieh, Wen Tsan Chang, Tzeng Horng Leu, Wen Chang Chang, Woei Jer Chuang, Ming Jer Tang, Tzong Yueh Chen, Te Ling Lu, Ming Derg Lai

研究成果: 雜誌貢獻文章

54 引文 (Scopus)

摘要

MST3 is a member of the sterile-20 protein kinase family with a unique preference for manganese ion as a cofactor in vitro; however, its biological function is largely unknown. Suppression of endogenous MST3 by small interference RNA enhanced cellular migration in MCF-7 cells with reduced expression of E-cadherin at the edge of migrating cells. The alteration of cellular migration and protruding can be rescued by RNA interference-resistant MST3. The expression of surface integrin and Golgi apparatus was not altered, but phosphorylation on tyrosine 118 and tyrosine 31 of paxillin was attenuated by MST3 small interfering RNA (siRNA). Threonine 178 was determined to be one of the two main autophosphorylation sites of MST3 in vitro. Mutant T178A MST3, containing alanine instead of threonine at codon 178, lost autophosphorylation and kinase activities. Overexpression of wild type MST3, but not the T178A mutant MST3, inhibited migration and spreading in Madin-Darby canine kidney cells. MST3 could phosphorylate the protein-tyrosine phosphatase (PTP)-PEST and inhibit the tyrosine phosphatase activity of PTP-PEST. We conclude that MST3 inhibits cell migration in a fashion dependent on autophosphorylation and may regulate paxillin phosphorylation through tyrosine phosphatase PTP-PEST.

原文英語
頁(從 - 到)38405-38417
頁數13
期刊Journal of Biological Chemistry
281
發行號50
DOIs
出版狀態已發佈 - 十二月 15 2006
對外發佈Yes

指紋

Cell Migration Inhibition
Paxillin
Protein Tyrosine Phosphatases
Tyrosine
Phosphorylation
Phosphotransferases
Cells
Threonine
RNA Interference
RNA
Phosphatases
Cadherins
Manganese
Phosphoric Monoester Hydrolases
Integrins
Alanine
Protein Kinases
Small Interfering RNA
Madin Darby Canine Kidney Cells
MCF-7 Cells

ASJC Scopus subject areas

  • Biochemistry

引用此文

Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST. / Lu, Te Jung; Lai, Wen Yang; Huang, Chi Ying F; Hsieh, Wan Jung; Yu, Jau Song; Hsieh, Ya Ju; Chang, Wen Tsan; Leu, Tzeng Horng; Chang, Wen Chang; Chuang, Woei Jer; Tang, Ming Jer; Chen, Tzong Yueh; Lu, Te Ling; Lai, Ming Derg.

於: Journal of Biological Chemistry, 卷 281, 編號 50, 15.12.2006, p. 38405-38417.

研究成果: 雜誌貢獻文章

Lu, TJ, Lai, WY, Huang, CYF, Hsieh, WJ, Yu, JS, Hsieh, YJ, Chang, WT, Leu, TH, Chang, WC, Chuang, WJ, Tang, MJ, Chen, TY, Lu, TL & Lai, MD 2006, 'Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST', Journal of Biological Chemistry, 卷 281, 編號 50, 頁 38405-38417. https://doi.org/10.1074/jbc.M605035200
Lu, Te Jung ; Lai, Wen Yang ; Huang, Chi Ying F ; Hsieh, Wan Jung ; Yu, Jau Song ; Hsieh, Ya Ju ; Chang, Wen Tsan ; Leu, Tzeng Horng ; Chang, Wen Chang ; Chuang, Woei Jer ; Tang, Ming Jer ; Chen, Tzong Yueh ; Lu, Te Ling ; Lai, Ming Derg. / Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST. 於: Journal of Biological Chemistry. 2006 ; 卷 281, 編號 50. 頁 38405-38417.
@article{67b0be6f576a446796870b95114622e6,
title = "Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST",
abstract = "MST3 is a member of the sterile-20 protein kinase family with a unique preference for manganese ion as a cofactor in vitro; however, its biological function is largely unknown. Suppression of endogenous MST3 by small interference RNA enhanced cellular migration in MCF-7 cells with reduced expression of E-cadherin at the edge of migrating cells. The alteration of cellular migration and protruding can be rescued by RNA interference-resistant MST3. The expression of surface integrin and Golgi apparatus was not altered, but phosphorylation on tyrosine 118 and tyrosine 31 of paxillin was attenuated by MST3 small interfering RNA (siRNA). Threonine 178 was determined to be one of the two main autophosphorylation sites of MST3 in vitro. Mutant T178A MST3, containing alanine instead of threonine at codon 178, lost autophosphorylation and kinase activities. Overexpression of wild type MST3, but not the T178A mutant MST3, inhibited migration and spreading in Madin-Darby canine kidney cells. MST3 could phosphorylate the protein-tyrosine phosphatase (PTP)-PEST and inhibit the tyrosine phosphatase activity of PTP-PEST. We conclude that MST3 inhibits cell migration in a fashion dependent on autophosphorylation and may regulate paxillin phosphorylation through tyrosine phosphatase PTP-PEST.",
author = "Lu, {Te Jung} and Lai, {Wen Yang} and Huang, {Chi Ying F} and Hsieh, {Wan Jung} and Yu, {Jau Song} and Hsieh, {Ya Ju} and Chang, {Wen Tsan} and Leu, {Tzeng Horng} and Chang, {Wen Chang} and Chuang, {Woei Jer} and Tang, {Ming Jer} and Chen, {Tzong Yueh} and Lu, {Te Ling} and Lai, {Ming Derg}",
year = "2006",
month = "12",
day = "15",
doi = "10.1074/jbc.M605035200",
language = "English",
volume = "281",
pages = "38405--38417",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "50",

}

TY - JOUR

T1 - Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST

AU - Lu, Te Jung

AU - Lai, Wen Yang

AU - Huang, Chi Ying F

AU - Hsieh, Wan Jung

AU - Yu, Jau Song

AU - Hsieh, Ya Ju

AU - Chang, Wen Tsan

AU - Leu, Tzeng Horng

AU - Chang, Wen Chang

AU - Chuang, Woei Jer

AU - Tang, Ming Jer

AU - Chen, Tzong Yueh

AU - Lu, Te Ling

AU - Lai, Ming Derg

PY - 2006/12/15

Y1 - 2006/12/15

N2 - MST3 is a member of the sterile-20 protein kinase family with a unique preference for manganese ion as a cofactor in vitro; however, its biological function is largely unknown. Suppression of endogenous MST3 by small interference RNA enhanced cellular migration in MCF-7 cells with reduced expression of E-cadherin at the edge of migrating cells. The alteration of cellular migration and protruding can be rescued by RNA interference-resistant MST3. The expression of surface integrin and Golgi apparatus was not altered, but phosphorylation on tyrosine 118 and tyrosine 31 of paxillin was attenuated by MST3 small interfering RNA (siRNA). Threonine 178 was determined to be one of the two main autophosphorylation sites of MST3 in vitro. Mutant T178A MST3, containing alanine instead of threonine at codon 178, lost autophosphorylation and kinase activities. Overexpression of wild type MST3, but not the T178A mutant MST3, inhibited migration and spreading in Madin-Darby canine kidney cells. MST3 could phosphorylate the protein-tyrosine phosphatase (PTP)-PEST and inhibit the tyrosine phosphatase activity of PTP-PEST. We conclude that MST3 inhibits cell migration in a fashion dependent on autophosphorylation and may regulate paxillin phosphorylation through tyrosine phosphatase PTP-PEST.

AB - MST3 is a member of the sterile-20 protein kinase family with a unique preference for manganese ion as a cofactor in vitro; however, its biological function is largely unknown. Suppression of endogenous MST3 by small interference RNA enhanced cellular migration in MCF-7 cells with reduced expression of E-cadherin at the edge of migrating cells. The alteration of cellular migration and protruding can be rescued by RNA interference-resistant MST3. The expression of surface integrin and Golgi apparatus was not altered, but phosphorylation on tyrosine 118 and tyrosine 31 of paxillin was attenuated by MST3 small interfering RNA (siRNA). Threonine 178 was determined to be one of the two main autophosphorylation sites of MST3 in vitro. Mutant T178A MST3, containing alanine instead of threonine at codon 178, lost autophosphorylation and kinase activities. Overexpression of wild type MST3, but not the T178A mutant MST3, inhibited migration and spreading in Madin-Darby canine kidney cells. MST3 could phosphorylate the protein-tyrosine phosphatase (PTP)-PEST and inhibit the tyrosine phosphatase activity of PTP-PEST. We conclude that MST3 inhibits cell migration in a fashion dependent on autophosphorylation and may regulate paxillin phosphorylation through tyrosine phosphatase PTP-PEST.

UR - http://www.scopus.com/inward/record.url?scp=33845989128&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33845989128&partnerID=8YFLogxK

U2 - 10.1074/jbc.M605035200

DO - 10.1074/jbc.M605035200

M3 - Article

C2 - 17046825

AN - SCOPUS:33845989128

VL - 281

SP - 38405

EP - 38417

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 50

ER -