Filamin A Phosphorylation at Serine 2152 by the Serine/Threonine Kinase Ndr2 Controls TCR-Induced LFA-1 Activation in T Cells

Front Immunol. 2018 Dec 4:9:2852. doi: 10.3389/fimmu.2018.02852. eCollection 2018.

Abstract

The integrin LFA-1 (CD11a/CD18) plays a critical role in the interaction of T cells with antigen presenting cells (APCs) to promote lymphocyte differentiation and proliferation. This integrin can be present either in a closed or in an open active conformation and its activation upon T-cell receptor (TCR) stimulation is a critical step to allow interaction with APCs. In this study we demonstrate that the serine/threonine kinase Ndr2 is critically involved in the initiation of TCR-mediated LFA-1 activation (open conformation) in T cells. Ndr2 itself becomes activated upon TCR stimulation and phosphorylates the intracellular integrin binding partner Filamin A (FLNa) at serine 2152. This phosphorylation promotes the dissociation of FLNa from LFA-1, allowing for a subsequent association of Talin and Kindlin-3 which both stabilize the open conformation of LFA-1. Our data suggest that Ndr2 activation is a crucial step to initiate TCR-mediated LFA-1 activation in T cells.

Keywords: Filamin A; Kindlin-3; LFA-1; Ndr2; T cells; TCR; Talin; inside-out signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • CD18 Antigens / immunology
  • CD18 Antigens / metabolism
  • Cells, Cultured
  • Cytoskeletal Proteins / immunology
  • Cytoskeletal Proteins / metabolism
  • Filamins / genetics
  • Filamins / immunology
  • Filamins / metabolism*
  • HEK293 Cells
  • Healthy Volunteers
  • Humans
  • Jurkat Cells
  • Lymphocyte Activation
  • Lymphocyte Function-Associated Antigen-1 / immunology
  • Lymphocyte Function-Associated Antigen-1 / metabolism*
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism
  • Mice
  • Mice, Knockout
  • Mutation
  • Neoplasm Proteins / immunology
  • Neoplasm Proteins / metabolism
  • Phosphorylation / immunology
  • Primary Cell Culture
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / immunology
  • Protein Serine-Threonine Kinases / metabolism*
  • Proteins / genetics
  • Proteins / metabolism*
  • Receptors, Antigen, T-Cell / immunology
  • Receptors, Antigen, T-Cell / metabolism*
  • Serine / metabolism
  • T-Lymphocytes / immunology*
  • T-Lymphocytes / metabolism
  • Talin / immunology
  • Talin / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • CD18 Antigens
  • Cytoskeletal Proteins
  • FERMT3 protein, human
  • FLNA protein, human
  • Filamins
  • FlnA protein, mouse
  • Lymphocyte Function-Associated Antigen-1
  • Membrane Proteins
  • Ndr2 protein, mouse
  • Neoplasm Proteins
  • Proteins
  • Receptors, Antigen, T-Cell
  • Talin
  • kindlin-3 protein, mouse
  • Serine
  • Protein Serine-Threonine Kinases
  • STK38L protein, human