Protein tyrosine phosphatases in signal transduction.
Protein-tyrosyl phosphorylation, regulated by protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is a key cellular control mechanism. Until recently, little was known about PTPs. However, the past two years have witnessed an explosion of information about PTP structure, regulation and function. Crystal structures of several PTPs have provided insights into enzymatic mechanisms and regulation and suggested the design of 'substrate-trapping' mutants. Candidate homophilic and heterophilic ligands for transmembrane PTPs have been identified, and roles for transmembrane PTPs in regulating cell-cell interactions have been suggested. Finally, progress has been made in understanding signaling by Src homology 2 domain containing PTPs and PTPs controlling yeast osmoregulatory pathways.
Neel
B G
BG
Cancer Biology Program, Division of Hematology-Oncology, Department of Medicine, HIM 1047, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA. bneel@bidmc.harvard.edu
Tonks
N K
NK
D000818:Animals; D002448:Cell Adhesion; D016207:Cytokines / Q000378:metabolism; D006133:Growth Substances / Q000378:metabolism; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D015398:Signal Transduction; D018909:src Homology Domains
D016207:Cytokines; D006133:Growth Substances; D011956:Receptors, Cell Surface; D011505:Protein-Tyrosine Kinases; D017027:Protein Tyrosine Phosphatases