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Phosphoprotein phosphatase inhibitor‐2 is phosphorylated at both serine and threonine residues in mouse diaphragm
Author(s) -
DePaoli-Roach Anna A.,
Lee Fook-Thean
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)80824-3
Subject(s) - phosphoserine , dusp6 , phosphatase , phosphorylation , phosphoprotein , serine , threonine , biochemistry , chemistry , microbiology and biotechnology , acid phosphatase , phosphate , in vivo , biology , protein phosphatase 2 , enzyme
Phosphoprotein phosphatase inhibitor‐2 (i‐2) was rapidly isolated from mouse diaphragm extracts by the use of specific antibodies. The i‐2 so obtained was associated with ATP‐Mg and F a /GSK‐3 dependent phosphatase activity, supporting the idea that i‐2 is in fact a component of this form of phosphatase. Inhibitor‐2 isolated from diaphragms incubated with [ 32 P]phosphate contained both phosphoserine (~ 90%) and phosphothreonine (~ 10%). Therefore, i‐2 is multiply phosphorylated in mouse diaphragm and the potential exists for control of the ATP‐Mg‐dependent phosphatase via multiple phosphorylation sites in vivo.