Premium
Dephosphorylation of the deinhibitor protein by the PCS H protein phosphatase
Author(s) -
Goris Jozef,
Waelkens Etienne,
Merlevede Wilfried
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80384-7
Subject(s) - dephosphorylation , phosphatase , phosphorylation , protein subunit , protein phosphatase 1 , protein kinase a , calcineurin , chemistry , biochemistry , enzyme , protein phosphatase 2 , microbiology and biotechnology , biology , medicine , transplantation , gene
The deinhibitor protein, responsible for the decreased sensitivity of the ATP, Mg‐dependent protein phosphatase to inhibitor‐1 and the modulator protein, is inactivated by cyclic AMP‐dependent protein kinase and reactivated by dephosphorylation. The specificity of this reaction was tested with the ATP, Mg‐dependent phosphatase in its activated or spontaneously active form, four different forms of polycation‐stimulated phosphatases (PCS H , PCS M , PCS L and PCS C ) and calcineurin. Only the high ‐ M r , polycation‐stimulated protein phosphatase (PCS H ), but not its catalytic subunit (PCS C ), shows a high degree of specificity for the deinhibitor protein. Deinhibitor phosphatase activity of PCS H is affected neither by polycations nor by Mn ions.