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p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins.

p62 is a novel cellular protein which was initially identified as a phosphotyrosine-independent ligand of the SH2 domain of p56(lck). In the yeast two-hybrid system, p62 specifically interacted with ubiquitin in vivo. Furthermore, p62 bound to ubiquitin-conjugated Sepharose beads in vitro and was efficiently competed by soluble ubiquitin. The interaction was independent of ATP hydrolysis, and its dissociation did not require a reducing agent. Thus, p62 binds to ubiquitin noncovalently. Further analysis showed that the C-terminal 80 amino acids of p62 were indispensable for its interaction with ubiquitin. However, p62 has homology neither with ubiquitin C-terminal hydrolases nor with the S5a subunit of the 26 S proteasome complex, the only proteins known to bind to ubiquitin noncovalently. These results suggest that p62 belongs to a new class of ubiquitin-binding proteins and that p62 affects signal transduction at least partly through ubiquitination-mediated protein degradation.

Pubmed ID: 8702753

Authors

  • Vadlamudi RK
  • Joung I
  • Strominger JL
  • Shin J

Journal

The Journal of biological chemistry

Publication Data

August 23, 1996

Associated Grants

  • Agency: NCI NIH HHS, Id: CA47554
  • Agency: NIGMS NIH HHS, Id: GM48961

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Binding Sites
  • Carrier Proteins
  • HeLa Cells
  • Humans
  • Immediate-Early Proteins
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
  • Protein Binding
  • Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Signal Transduction
  • Ubiquitins
  • src Homology Domains
  • src-Family Kinases