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Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130.

It has previously been reported that in resting T-lymphocytes the protein tyrosine kinase p59 constitutively co-precipitates with four phosphoproteins of 43, 55, 85, and 120 kDa, respectively. We have recently cloned the 55-kDa protein that was termed Src kinase-associated phosphoprotein of 55 kDa (SKAP55). Here we demonstrate that the recently characterized SH2-domain-containing leukocyte protein 76-associated phosphoprotein of 130 kDa (SLAP-130) is one of the components of the Fyn complex and that it also co-precipitates with SKAP55 in human T-cells. We establish that SKAP55 and SLAP-130 associate with each other when both molecules are co-expressed in COS cells. By co-transfection of truncated mutants of SKAP55 and SLAP-130 as well as by using the two-hybrid selection system, we further demonstrate that the association between SLAP-130 and SKAP55 is direct and involves the Src homology 3 domain of SKAP55 and the proline-rich sequence of SLAP-130.

Pubmed ID: 9748251


  • Marie-Cardine A
  • Hendricks-Taylor LR
  • Boerth NJ
  • Zhao H
  • Schraven B
  • Koretzky GA


The Journal of biological chemistry

Publication Data

October 2, 1998

Associated Grants

  • Agency: NIAID NIH HHS, Id: 2T32 AI07260
  • Agency: NIGMS NIH HHS, Id: R01 GM53256

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Carrier Proteins
  • Cloning, Molecular
  • Humans
  • Jurkat Cells
  • Mutation
  • Oligopeptides
  • Peptides
  • Phosphoproteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-fyn
  • Signal Transduction
  • Transfection
  • src Homology Domains