Combinatorial control of the specificity of protein tyrosine phosphatases.
Protein tyrosine phosphatases (PTPs), the enzymes that dephosphorylate tyrosyl phosphoproteins, were initially believed to be few in number and serve a 'housekeeping' role in signal transduction. Recent work indicates that this is totally incorrect. Instead, PTPs comprise a large superfamily whose members play critical roles in a wide variety of cellular processes. Moreover, PTPs exhibit exquisite substrate specificity in vivo. Recent evidence has led us to propose that members of the PTP family achieve selectivity through different combinations of specific targeting strategies and intrinsic catalytic domain specificity.
Tonks
N K
NK
Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, New York 11724, USA. tonks@cshl.org
Neel
B G
BG
D000818:Animals; D006801:Humans; D017434:Protein Structure, Tertiary; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D015398:Signal Transduction; D013379:Substrate Specificity
D017027:Protein Tyrosine Phosphatases