The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large

J Biol Chem. 2004 Aug 6;279(32):33816-28. doi: 10.1074/jbc.M401040200. Epub 2004 May 11.

Abstract

Clustering of the T cell integrin, LFA-1, at specialized regions of intercellular contact initiates integrin-mediated adhesion and downstream signaling, events that are necessary for a successful immunological response. But how clustering is achieved and sustained is not known. Here we establish that an LFA-1-associated molecule, PTA-1, is localized to membrane rafts and binds the carboxyl-terminal domain of isoforms of the actin-binding protein 4.1G. Protein 4.1 is known to associate with the membrane-associated guanylate kinase homologue, human discs large. We show that the carboxyl-terminal peptide of PTA-1 also can bind human discs large and that the presence or absence of this peptide greatly influences binding between PTA-1 and different isoforms of 4.1G. T cell stimulation with phorbol ester or PTA-1 cross-linking induces PTA-1 and 4.1G to associate tightly with the cytoskeleton, and the PTA-1 from such activated cells now can bind to the amino-terminal region of 4.1G. We propose that these dynamic associations provide the structural basis for a regulated molecular adhesive complex that serves to cluster and transport LFA-1 and associated molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Antigens, Differentiation, T-Lymphocyte / chemistry*
  • Antigens, Differentiation, T-Lymphocyte / genetics
  • Antigens, Differentiation, T-Lymphocyte / metabolism*
  • Binding Sites
  • Biological Transport
  • CHO Cells
  • Cell Membrane / chemistry
  • Cell Membrane / ultrastructure
  • Cricetinae
  • Cross-Linking Reagents
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeleton / metabolism
  • Discs Large Homolog 1 Protein
  • Glutathione Transferase / genetics
  • Humans
  • Jurkat Cells
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Isoforms / metabolism
  • Proteins / chemistry
  • Proteins / metabolism*
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae / genetics
  • T-Lymphocytes / chemistry*
  • Transfection
  • Two-Hybrid System Techniques

Substances

  • Adaptor Proteins, Signal Transducing
  • Antigens, Differentiation, T-Lymphocyte
  • CD226 antigen
  • Cross-Linking Reagents
  • Cytoskeletal Proteins
  • DLG1 protein, human
  • Discs Large Homolog 1 Protein
  • Membrane Proteins
  • Protein Isoforms
  • Proteins
  • Recombinant Fusion Proteins
  • erythrocyte membrane band 4.1 protein
  • Glutathione Transferase