scholarly journals The nonconserved N-terminus of protein phosphatase 2B confers its properties to protein phosphatase 1

IUBMB Life ◽  
2009 ◽  
Vol 61 (2) ◽  
pp. 178-183 ◽  
Author(s):  
Xiu-Jie Xie ◽  
Wei Huang ◽  
Cheng-Zhe Xue ◽  
Qun Wei
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Protein Phosphatase 2B ◽  
N Terminus

scholarly journals Protein phosphatase 2A is a specific protamine-kinase-inactivating phosphatase

1992 ◽  
Vol 287 (3) ◽  
pp. 1019-1022 ◽  
Author(s):  
G D Amick ◽  
S A G Reddy ◽  
Z Damuni
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Protein Phosphatase ◽  
Kinase Activity ◽  
Protein Phosphatase 2A ◽  
Tyrosine Phosphatase ◽  
Protein Phosphatase 1 ◽  
Protein Phosphatase 2B ◽  
2B Protein ◽  
Phosphatase 2A ◽  
Protamine Kinase

Purified preparations of a protamine protein kinase from bovine kidney cytosol [Damuni, Amick & Sneed (1989) J. Biol. Chem. 264, 6412-6416] were inactivated after incubation with near-homogeneous preparations of protein phosphatase 2A1 and protein phosphatase 2A2. These protein phosphatase 2A-mediated inactivations of the protamine kinase were unaffected by highly purified preparations of inhibitor 2, but were prevented when the incubations were performed in the presence of 100 nM microcystin-LR, 100 nM okadaic acid or 0.2 mM-ATP. By contrast, highly purified preparations of protein phosphatase 2B, protein phosphatase 2C, the catalytic subunit of protein phosphatase 1, and two forms of a protein tyrosine phosphatase, designated PTPase 1B and T-cell PTPase, had little effect, if any, on protamine kinase activity. Purified preparations of the protamine kinase did not react with anti-phosphotyrosine antibodies, as determined by Western blotting and immunoprecipitation analysis. The results indicate that protein phosphatase 2A is a specific protamine-kinase-inactivating phosphatase.

Detection of multiple splice variants of the nuclear protein phosphatase 1 regulator sds22 in rat liver nuclei

2002 ◽  
Vol 80 (6) ◽  
pp. 811-815 ◽  
Author(s):  
Hue T Tran ◽  
Dave Bridges ◽  
Annegret Ulke ◽  
Greg B.G Moorhead
Keyword(s):  
Rat Liver ◽  
Protein Phosphatase ◽  
Nuclear Protein ◽  
Splice Variants ◽  
Nuclear Extract ◽  
Nuclear Proteins ◽  
Protein Phosphatase 1 ◽  
N Terminus ◽  
Liver Nuclei ◽  
Different Levels

Antipeptide antibodies generated against the N terminus of the protein phosphatase 1 (PP1) binding protein sds22 detected at least four forms of the protein in a rat liver nuclear extract. Four of these immunoreactive bands likely correspond to four predicted forms of sds22 that are generated by alternative splicing. These four proteins are expressed at different levels and appear to be localized exclusively in the nucleus, and two of these proteins copurify with PP1 on the protein phosphatase affinity matrix microcystin–Sepharose. Two higher molecular mass nuclear proteins that are immunoreactive with the sds22 antibodies also copurify on microcystin–Sepharose and may be novel forms of sds22 expressed in mammalian cells.Key words: sds22, protein phosphatase 1 (PP1), nucleus, microcystin–Sepharose.

Regulation of glycogen synthase and protein phosphatase-1 by hexosamines

Diabetes ◽  
1996 ◽  
Vol 45 (3) ◽  
pp. 322-327 ◽  
Author(s):  
E. D. Crook ◽  
D. A. McClain
Keyword(s):  
Protein Phosphatase ◽  
Glycogen Synthase ◽  
Protein Phosphatase 1
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