Altered substrate selectivity of PKC-eta pseudosubstrate site mutants.
Three protein kinase C (PKC)-eta mutants were constructed in which the whole or part of the pseudosubstrate site was replaced with corresponding parts of the PKC-alpha pseudosubstrate site. The resulting chimaeric kinases were compared with wild-type PKC-eta in their ability to phosphorylate a PKC-eta peptide substrate or histone. Changes in the pseudosubstrate site of PKC-eta are accompanied by changes in substrate selectivity, indicating that the substrate selectivity observed for PKC-eta is at least in part due to its pseudosubstrate site.
Dekker
L V
LV
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, London, UK.
McIntyre
P
P
Parker
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005590:Fractional Precipitation; D006657:Histones / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D006657:Histones; D010455:Peptides; D011493:Protein Kinase C