Regulation of Tyrosine Protein Phosphatases by Binding to Phospholipids and Covalent Modification
The regulation of the phosphorylation state of tyrosine residues in proteins is of pivotal importance for the transduction of growth factor signals, cellular growth and differentiation as well as for the suppression of tumour formation. Protein phosphatases are involved in these processes in a dual mode by regulating the activity of some serine/threonine- and tyrosine-specific protein kinases and by counteracting phosphorylation of proteins by tyrosine kinases. The majority of the tyrosine phosphatases so far identified exhibit sequence homology within their catalytic domains and can be attributed to two different subfamilies (reviewed in 1,2): The members of the receptor phosphatase subfamily contain a transmembrane domain and extracellular domains with similarities to cell adhesion molecules or immunoglobulins and (with one known exception) two catalytic domains (see Ref. 3). Most, if not all, members of this subfamily are integral membrane proteins. A second subfamily is formed by tyrosine phosphatases consisting of a single catalytic domain. Though they are not comprising a transmembrane sequence, they have nevertheless also been reported to associate with membranes or other particulate cellular compartments (4–6).
KeywordsAttenuation Tyrosine Heparin Serine Choline
reduced carboxymethylated and maleylated lysozyme
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