Abstract:
:PTP1C, a protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) containing two src homology 2 domains, is poorly active when assayed with various protein substrates in vitro. Its activity is stimulated > 1000-fold by anionic phospholipids when myelin basic protein or mitogen-activated protein kinase is used as substrate but reduced in the presence of several other substrates. Data are presented to indicate a direct interaction of the enzyme with phospholipids. Enzyme stimulation directed only toward certain specific substrates is interpreted by assuming that these compounds also bind to the phospholipid vesicles where they will be subjected to rapid enzymatic attack. A possible regulation of PTP1C by its translocation to the cell membrane is hypothesized.
journal_name
Proc Natl Acad Sci U S Aauthors
Zhao Z,Shen SH,Fischer EHdoi
10.1073/pnas.90.9.4251subject
Has Abstractpub_date
1993-05-01 00:00:00pages
4251-5issue
9eissn
0027-8424issn
1091-6490journal_volume
90pub_type
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