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Mst1 directs Myosin IIa partitioning of low and higher affinity integrins during T cell migration

Academic Article
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Overview

authors

  • Xu, X.
  • Jaeger, E. R.
  • Wang, X.
  • Lagler-Ferrez, E.
  • Batalov, S.
  • Mathis, N. L.
  • Wiltshire, T.
  • Walker, J. R.
  • Cooke, M. P.
  • Sauer, Karsten
  • Huang, Y. H.

publication date

  • August 2014

journal

  • PLoS One  Journal

abstract

  • Chemokines promote T cell migration by transmitting signals that induce T cell polarization and integrin activation and adhesion. Mst1 kinase is a key signal mediator required for both of these processes; however, its molecular mechanism remains unclear. Here, we present a mouse model in which Mst1 function is disrupted by a hypomorphic mutation. Microscopic analysis of Mst1-deficient CD4 T cells revealed a necessary role for Mst1 in controlling the localization and activity of Myosin IIa, a molecular motor that moves along actin filaments. Using affinity specific LFA-1 antibodies, we identified a requirement for Myosin IIa-dependent contraction in the precise spatial distribution of low and higher affinity LFA-1 on the membrane of migrating T cells. Mst1 deficiency or Myosin inhibition resulted in multipolar cells, difficulties in uropod detachment and mis-localization of low affinity LFA-1. Thus, Mst1 regulates Myosin IIa dynamics to organize high and low affinity LFA-1 to the anterior and posterior membrane during T cell migration.

subject areas

  • Animals
  • Cell Movement
  • Cells, Cultured
  • Chemokine CCL19
  • Hepatocyte Growth Factor
  • Integrins
  • Lymphocyte Function-Associated Antigen-1
  • Mice, Inbred C57BL
  • Mutation
  • Nonmuscle Myosin Type IIA
  • Proto-Oncogene Proteins
  • T-Lymphocytes
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Identity

PubMed Central ID

  • PMC4136924

International Standard Serial Number (ISSN)

  • 1932-6203

Digital Object Identifier (DOI)

  • 10.1371/journal.pone.0105561

PubMed ID

  • 25133611
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Additional Document Info

start page

  • e105561

volume

  • 9

issue

  • 8

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