Studies on the primary sequence requirements for PKC-alpha, -beta 1 and -gamma peptide substrates.
The substrate specificity of purified PKC-alpha, -beta and -gamma has been investigated. A series of synthetic peptides based upon the sequence surrounding serine-7 in glycogen synthase were generated and used to determine the basic residue requirements of these PKC isotypes. While PKC-alpha and -beta are indistinguishable in their phosphorylation of these peptides, PKC-gamma shows a distinct specificity profile for these synthetic substrates.
Marais
R M
RM
Ludwig Institute for Cancer Research, London, UK.
Nguyen
O
O
Woodgett
J R
JR
Parker
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D066246:ErbB Receptors / Q000378:metabolism; D006006:Glycogen Synthase / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D016392:Proto-Oncogene Proteins pp60(c-src) / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004676:Myelin Basic Protein; D010455:Peptides; D006006:Glycogen Synthase; D066246:ErbB Receptors; D016392:Proto-Oncogene Proteins pp60(c-src); D011493:Protein Kinase C