In:
FEBS Letters, Wiley, Vol. 207, No. 1 ( 1986-10-20), p. 167-172
Abstract:
The phosphorylation by casein kinase TS (II) of the modulator protein of the ATP,Mg‐dependent phosphatase increases after preineubation with the PCS H1 phosphatase or with the catalytic subunit of the ATP,Mg‐dependent phosphatase. Dephosphorylation by the two phosphatases combined leads to the incorporation of 2 mol phosphate per mol modulator (at Ser residues). Occupancy of the ATP,Mg‐dependent phosphatase phosphorylation site(s) is a negative determinant in the phosphorylation of the modulator by kinase TS. Among the PCS phosphatases PCS h1 shows the highest activity toward the 32 P‐Ser residues labeled by kinase TS in untreated or previously dephosphorylated modulator, while the ATP,Mg‐dependent phosphatase is totally ineffective. Protamine stimulates all phosphatase activities, so that the catalytic subunit of the ATP,Mg‐dependent phosphatase becomes almost as effective as the PCS C phosphatase in dephosphorylating the kinase TS sites.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(86)80033-3
Language:
English
Publisher:
Wiley
Publication Date:
1986
detail.hit.zdb_id:
1460391-3
SSG:
12
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