Tyrosine Phosphorylation of Paxillin during Cell Adhesion

Jong Soo Chang, Hongmie Lee, Do Sik Min

Research output: Contribution to journalArticle

Abstract

Proteins that are involved in cellular signal cascade experience phosphorylation and dephosphorylation cycles in their tyrosine residue(s) during cell adhesion. In order to identify the protein(s), which tyrosine desidues are specifically phosphorylated when the cells attached to the substrate, we compared the tyrosine phosphorylation level of proteins between suspension and adhered culture condition in rat fibroblast 3Y1 cells. We found that a cluster of 70 kDa protein was specifically phosphorylated when the cells adhered to the substrate, but did not effect the cells held in suspension. The phosphorylated protein is identified as paxillin, a focal adhesion protein in immunoprecipitation and immunobloting analysis. These results suggest that the tyrosine phosphorylation of paxillin may play a role in cell-substrate adhesion.

Original languageEnglish
Pages (from-to)349-352
Number of pages4
JournalJournal of Biochemistry and Molecular Biology
Volume33
Issue number4
Publication statusPublished - 2000 Jul 31

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Paxillin
Phosphorylation
Cell adhesion
Cell Adhesion
Tyrosine
Proteins
Suspensions
Substrates
Adhesion
Focal Adhesions
Fibroblasts
Cell culture
Immunoprecipitation
Rats

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

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Tyrosine Phosphorylation of Paxillin during Cell Adhesion. / Chang, Jong Soo; Lee, Hongmie; Min, Do Sik.

In: Journal of Biochemistry and Molecular Biology, Vol. 33, No. 4, 31.07.2000, p. 349-352.

Research output: Contribution to journalArticle

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