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

FEBS letters ·Vol. 277 ·No. 1-2 ·1990-12-17 ·Pages 151-5

Marais RM, Nguyen O, Woodgett JR, Parker PJ

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,metabolism Protein Kinase C/metabolism Proto-Oncogene Proteins pp60(c-src)/metabolism Structure-Activity Relationship Substrate Specificity

Chemicals

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

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Marais R M

Ludwig Institute for Cancer Research, London, UK.

Nguyen O

Woodgett J R

Parker P J

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(90)80831-3

Published

1990-12-17

Pages

151-5

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(90)80831-3 View journal details

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

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