In:
FEBS Letters, Wiley, Vol. 554, No. 3 ( 2003-11-20), p. 253-256
Abstract:
Inhibitor‐2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase‐1 (PP1), resulting in the formation of the inactive holoenzyme, ATP‐Mg‐dependent phosphatase. Phosphorylation of I2 at Thr‐72 by glycogen synthase kinase‐3 (GSK‐3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK‐3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP‐Mg‐dependent phosphatase induced by GSK‐3 phosphorylation must depend on the interactions between PP1 and I2.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(03)01097-4
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
1460391-3
SSG:
12
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