'Zip codes' direct intracellular protein tyrosine phosphatases to the correct cellular 'address'.
The transmembrane and intracellular protein tyrosine phosphatases (PTPs) play an essential role as signal transduction proteins involved in various cellular processes including division, proliferation and differentiation. As such, their activity must be strictly regulated to avoid nonspecific tyrosine dephosphorylation of cellular proteins. The intracellular PTPs possess a diversity of protein sequences outside the catalytic domain that appear to serve as 'zip codes' specifically 'addressing' these proteins to defined subcellular compartments. These localization strategies are proposed to function as a regulatory mechanism, defining the substrate specificity and function of the intracellular PTPs.
Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor 48109.
L J
LJ
Mauro
J E
JE
Dixon
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002467:Cell Nucleus / Q000201:enzymology; D003599:Cytoskeleton / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000378:metabolism
D013438:Sulfhydryl Compounds; D017027:Protein Tyrosine Phosphatases