Protein Tyrosine Phosphatases: The Problems of a Growing Family

  1. N.K. Tonks,
  2. Q. Yang,
  3. A.J. Flint,
  4. M.F.B.G. Gebbink,
  5. B.R. Franza, Jr.*,
  6. D.E. Hill,
  7. H. Sun, and
  8. S. Brady-Kalnay
  1. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; *Freeman Laboratory of Cancer Cell Biology, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; Applied Biotechnology, Inc., Cambridge, Massachusetts 02138

This extract was created in the absence of an abstract.

Excerpt

Protein tyrosine phosphorylation is now recognized as an important component of the control of many fundamental aspects of cellular function, including growth and differentiation, cell cycle and cytoskeletal integrity. In vivo, the net level of phosphorylation of tyrosyl residues in a target substrate reflects the balance between the competing action of kinases and phosphatases. We are examining physiological roles for protein tyrosine phosphorylation, pursuing the problem from the perspective of the enzymes that catalyze the dephosphorylation reaction, the protein tyrosine phosphatases (PTPases). The PTPases have, until recently, been somewhat neglected relative to the protein tyrosine kinases (PTKs). However, considerable progress has been made in identifying new members of the PTPase family, and it appears that they constitute a novel class of signal transducing molecules that rival the PTKs in their structural diversity and complexity.

One of the principal reasons that the study of PTPases has lagged behind that of the...

| Table of Contents