Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1

1993 ◽  
Vol 127-128 (1) ◽  
pp. 113-119 ◽  
Author(s):  
Zhongjian Zhang ◽  
Sumin Zhao ◽  
Stephen Deans-Zirattu ◽  
Ge Bai ◽  
Ernest Y. C. Lee
Keyword(s):  
Protein Phosphatase ◽  
Muscle Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Rabbit Muscle

Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1

1993 ◽  
pp. 113-119
Author(s):  
Zhongjian Zhang ◽  
Sumin Zhao ◽  
Stephen Deans-Zirattu ◽  
Ge Bai ◽  
Ernest Y. C. Lee
Keyword(s):  
Protein Phosphatase ◽  
Muscle Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Rabbit Muscle

Mutational Analysis of the Catalytic Subunit of Muscle Protein Phosphatase-1†

Biochemistry ◽  
1996 ◽  
Vol 35 (20) ◽  
pp. 6276-6282 ◽  
Author(s):  
Jun Zhang ◽  
Zhongjian Zhang ◽  
Keith Brew ◽  
Ernest Y. C. Lee
Keyword(s):  
Protein Phosphatase ◽  
Mutational Analysis ◽  
Muscle Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1

scholarly journals A cDNA encoding rabbit muscle protein phosphatase 1 alpha complements the Aspergillus cell cycle mutation, bimG11.

1991 ◽  
Vol 266 (28) ◽  
pp. 18889-18894
Author(s):  
J.H. Doonan ◽  
C. MacKintosh ◽  
S. Osmani ◽  
P. Cohen ◽  
G. Bai ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Phosphatase ◽  
Muscle Protein ◽  
Protein Phosphatase 1 ◽  
Rabbit Muscle

scholarly journals The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein

2002 ◽  
Vol 365 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Isabel MAYORDOMO ◽  
Pascual SANZ
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Regulation ◽  
Intermediate Filament ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Intermediate Filament Protein ◽  
Filament Protein ◽  
Two Hybrid ◽  
Hybrid Screening

In order to identify proteins that interact with Bmh2, a yeast member of the 14-3-3 protein family, we performed a two-hybrid screening using LexA-Bmh2 as bait. We identified Fin1, a novel intermediate filament protein, as the protein that showed the highest degree of interaction. We also identified components of the vesicular transport machinery such as Gic2 and Msb3, proteins involved in transcriptional regulation such as Mbf1, Gcr2 and Reg2, and a variety of other different proteins (Ppt1, Lre1, Rps0A and Ylr177w). We studied the interaction between Bmh2 and Fin1 in more detail and found that Bmh2 only interacted with phosphorylated forms of Fin1. In addition, we showed that Glc7, the catalytic subunit of the protein phosphatase 1 complex, was also able to interact with Fin1.

scholarly journals Full activation of a nuclear species of protein phosphatase-1 by phosphorylation with protein kinase A and casein kinase-2

1994 ◽  
Vol 297 (3) ◽  
pp. 447-449 ◽  
Author(s):  
A Van Eynde ◽  
M Beullens ◽  
W Stalmans ◽  
M Bollen
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Fold Increase ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Nuclear Species ◽  
Kinase A

Bovine thymus nuclei contain a species of protein phosphatase-1 (PP-1N alpha) that can be partially activated by phosphorylation of an associated inhibitory polypeptide, NIPP-1, with protein kinase A [Beullens, Van Eynde, Bollen and Stalmans (1993) J. Biol. Chem. 268, 13172-13177]. Here it is shown that PP-1N alpha can also be activated 4-fold by phosphorylation of NIPP-1 with casein kinase-2. The effects of protein kinase A and casein kinase-2 were additive, yielding an enzyme with an activity close to that of the free catalytic subunit. Casein kinase-2 introduced up to 1.2 phosphate groups into purified NIPP-1 on serine and threonine residues. This phosphorylation was associated with a 14-fold increase in the concentration of NIPP-1 required for 50% inhibition of the type-1 catalytic subunit. The kinase-mediated inactivation of NIPP-1 could be reversed by incubation with the catalytic subunit of protein phosphatase-2A.

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