LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin

Cancer Science
Toshiyuki TanakaMasayuki Miyasaka

Abstract

Focal adhesion (FA) consists of multiple cellular proteins including paxillin and serves as a center for adhesion-mediated signaling. The assembly and disassembly of FAs is regulated by locally produced intracellular signals, and tyrosine phosphorylation of paxillin has been implicated in this process. A Lin-11 Isl-1 Mec-3 (LIM) domain-containing adaptor protein, leupaxin, a member of the paxillin family, is expressed in leukocytes as well as in certain cancer cells, and shares overall structural characteristics with paxillin. However, it remains unknown whether leupaxin and paxillin cooperate with or antagonize each other in integrin signaling. Here we show that leupaxin potently represses the tyrosine phosphorylation of paxillin. When expressed in mouse thymoma BW5147 cells bound to ICAM-1, leupaxin accumulated in FA-like patches in the cell periphery. When expressed in NIH3T3 and HEK293T cells, leupaxin localized to FAs upon cell adhesion to fibronectin and strongly suppressed the integrin-induced tyrosine phosphorylation of paxillin. In integrin-stimulated HEK293T cells, leupaxin's LIM3 domain appeared essential for selective FA localization and the suppression of paxillin tyrosine phosphorylation. Leupaxin's LD3 motif, whi...Continue Reading

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Citations

Dec 12, 2012·Genes & Cancer·Nicholas O DeakinChristopher E Turner
Jun 21, 2015·Progress in Biophysics and Molecular Biology·Katarzyna W WalkiewiczStefan T Arold
Nov 3, 2016·PloS One·Andrew E JacobJeffrey D Amack
Sep 21, 2019·The Journal of Cell Biology·Sarah KlapprothMarkus Moser
Apr 10, 2020·Frontiers in Immunology·Amélie BonaudMarion Espéli
Sep 11, 2012·The American Journal of Pathology·Christine VeithGrażyna Kwapiszewska
Jun 13, 2021·Journal of Molecular and Cellular Cardiology·Xinming WangSamuel E Senyo
Nov 5, 2021·Clinical Epigenetics·Gesa M RichterArne S Schaefer

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