PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration

Yun Ju Lai, Weei Chin Lin, Fang Tsyr Lin

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The LIM domain-containing TRIP6 (Thyroid Hormone Receptor-interacting Protein 6) is a focal adhesion molecule known to regulate lysophosphatidic acid (LPA)-induced cell migration through interaction with the LPA2 receptor. LPA stimulation targets TRIP6 to the focal adhesion complexes and promotes c-Src-dependent phosphorylation of TRIP6 at Tyr-55, which creates a docking site for the Crk Src homology 2 domain, thereby promoting LPA-induced morphological changes and cell migration. Here we further demonstrate that a switch from c-Src-mediated phosphorylation to PTPL1/Fas-associated phosphatase-1-dependent dephosphorylation serves as an inhibitory feedback control mechanism of TRIP6 function in LPA-induced cell migration. PTPL1 dephosphorylates phosphotyrosine 55 of TRIP6 in vitro and inhibits LPA-induced tyrosine phosphorylation of TRIP6 in cells. This negative regulation requires a direct protein-protein interaction between these two molecules and the phosphatase activity of PTPL1. In contrast to c-Src, PTPL1 prevents TRIP6 turnover at the sites of adhesions. As a result, LPA-induced association of TRIP6 with Crk and the function of TRIP6 to promote LPA-induced morphological changes and cell migration are inhibited by PTPL1. Together, these results reveal a novel mechanism by which PTPL1 phosphatase plays a counteracting role in regulating TRIP6 function in LPA-induced cell migration.

Original languageEnglish
Pages (from-to)24381-24387
Number of pages7
JournalJournal of Biological Chemistry
Volume282
Issue number33
DOIs
Publication statusPublished - 2007 Aug 17

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Cell Movement
Phosphorylation
Phosphoric Monoester Hydrolases
Focal Adhesions
Adhesion
Lysophosphatidic Acid Receptors
thyroid-hormone-receptor interacting protein
lysophosphatidic acid
Phosphotyrosine
Molecules
src Homology Domains
Feedback control
Tyrosine
Proteins
Switches
Association reactions

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration. / Lai, Yun Ju; Lin, Weei Chin; Lin, Fang Tsyr.

In: Journal of Biological Chemistry, Vol. 282, No. 33, 17.08.2007, p. 24381-24387.

Research output: Contribution to journalArticle

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