[HTML][HTML] p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
RK Vadlamudi, I Joung, JL Strominger, J Shin - Journal of Biological …, 1996 - ASBMB
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 …
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 …