Studies on the primary sequence requirements for PKC-alpha, -beta 1 and -gamma peptide substrates

R M Marais; O Nguyen; J R Woodgett; P J Parker

doi:10.1016/0014-5793(90)80831-3

Studies on the primary sequence requirements for PKC-alpha, -beta 1 and -gamma peptide substrates

FEBS Lett. 1990 Dec 17;277(1-2):151-5. doi: 10.1016/0014-5793(90)80831-3.

Authors

R M Marais¹, O Nguyen, J R Woodgett, P J Parker

Affiliation

¹ Ludwig Institute for Cancer Research, London, UK.

PMID: 1702730
DOI: 10.1016/0014-5793(90)80831-3

Abstract

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.

MeSH terms

Amino Acid Sequence
Animals
Cattle
ErbB Receptors / metabolism
Glycogen Synthase / metabolism
In Vitro Techniques
Kinetics
Molecular Sequence Data
Myelin Basic Protein / metabolism
Peptides / chemistry
Peptides / metabolism
Protein Kinase C / metabolism*
Proto-Oncogene Proteins pp60(c-src) / metabolism
Structure-Activity Relationship
Substrate Specificity

Substances

Myelin Basic Protein
Peptides
Glycogen Synthase
ErbB Receptors
Proto-Oncogene Proteins pp60(c-src)
Protein Kinase C