scholarly journals Identification of three in vivo phosphorylation sites on the glycogen-binding subunit of protein phosphatase 1 from rabbit skeletal muscle, and their response to adrenaline

FEBS Letters ◽  
1990 ◽  
Vol 259 (2) ◽  
pp. 281-285 ◽  
Author(s):  
Paul Dent ◽  
David G. Campbell ◽  
F.Barry Caudwell ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Protein Phosphatase ◽  
Rabbit Skeletal Muscle ◽  
Protein Phosphatase 1 ◽  
Phosphorylation Sites ◽  
Binding Subunit

scholarly journals Disruption of the striated muscle glycogen-targeting subunit of protein phosphatase 1: influence of the genetic background

2007 ◽  
Vol 40 (2) ◽  
pp. 47-59 ◽  
Author(s):  
James Paterson ◽  
Ian R Kelsall ◽  
Patricia T W Cohen
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Muscle Glycogen ◽  
Protein Phosphatase ◽  
Striated Muscle ◽  
Protein Phosphatase 1 ◽  
Phosphorylase Kinase ◽  
Donor Strain ◽  
Key Factor

A prediabetic phenotype of glucose intolerance, insulin resistance and obesity was observed at ∼12 months of age in mice homozygous for a null allele of the major skeletal muscle glycogen-targeting subunit GM of protein phosphatase 1 (PP1) and derived from a 129/Ola donor strain. In this study, backcrossing of these mice (termed obese mice) onto two different genetic backgrounds gave rise to lean, glucose-tolerant, insulin-sensitive mice (termed lean mice), indicating that at least one variant gene in the 129/Ola background, not present in the C57BL/6 or 129s2/sV background, is required for the development of the prediabetic phenotype of obese mice. Slightly elevated AMP-activated protein kinase α2 activity in the skeletal muscle of lean C57BL/6 mice was also observed to a lesser extent in the obese mice. Normal or slightly raised in vivo glucose transport in lean C57BL/6 mice compared with decreased glucose transport in the obese mice supports the tenet that adequate transport of glucose may be a key factor in preventing the development of the prediabetic phenotype. The pH 6.8/pH 8.6 activity ratio of phosphorylase kinase was increased in lean C57BL/6 mice compared with controls indicating that phosphorylase kinase is an in vivo substrate of PP1-GM.

Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17

2003 ◽  
Vol 302 (2) ◽  
pp. 186-192 ◽  
Author(s):  
Thierry Dubois ◽  
Steven Howell ◽  
Eva Zemlickova ◽  
Michele Learmonth ◽  
Andy Cronshaw ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Phosphorylation Sites
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