Deletion analysis of protein kinase Calpha reveals a novel regulatory segment.

Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Research Abstract Details 

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Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Abstract Text:

S A Rotenberg,J Zhu,H Hansen,X D Li,X G Sun,C A Michels,H Riedel,

Using a combined pharmacological and genetic approach, we have identified aa 260-280 in the C2 region as a critical factor in the catalytic function of protein kinase Calpha (PKCalpha). Progressive truncations from the N-terminus as well as selected internal deletion mutants were expressed in Saccharomyces cerevisiae and tested for altered sensitivity to dequalinium, a PKC inhibitor whose target site was previously mapped to the catalytic domain. PKC mutants representing truncations of up to 158 amino acid residues (aa) from the N-terminus (ND84 and ND158) displayed 60-63% inhibition of kinase activity by 50 microM dequalinium, somewhat more sensitive than the wild-type PKCalpha enzyme (45% inhibition). Mutant ND262, lacking N-terminal aa 1-262, was inhibited by almost 72% with 50 microM dequalinium, but mutant ND278, which lacked an additional 16 aa, was inhibited by only 9% of total activity. This result suggests that a C-terminal segment of the C2 region (aa 263-278) influences inhibition by dequalinium at low micromolar concentrations. An internal deletion mutant (D260-280) which retains the entire primary structure of PKCalpha except for aa 260-280, was similarly inhibited by only 4% with 50 microM dequalinium. In the absence of dequalinium and despite the presence of a nearly complete regulatory domain, this mutant exhibited constitutive activity (both in vitro and in a phenotypic assay with S. cerevisiae) that could not be further stimulated even by the potent activator TPA. Taken together, our findings suggest that, in the native structure of PKCalpha, the segment described by aa 260-280 regulates PKCalpha activity and influences the sensitivity of PKCalpha to dequalinium.

Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Publishing Authors By Initials

SA Rotenberg,J Zhu,H Hansen,XD Li,XG Sun,CA Michels,H Riedel,

For similar genetic processes: mutagenesis: sequence deletion research abstracts see: genetic processes: mutagenesis: sequence deletion research

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Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of biochemistry

VOLUME: 124

Page Numbers: 756-63

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1998

Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Keywords Mesh Terms:

KEYWORDS: Sequence Deletion

MESH TERMS: metabolism

Chemical & Substance for Abstract: Deletion analysis of protein kinase Calpha reveals a novel regulatory segment. Information

Substance Name: Protein Kinase C

Registry Number: EC 2.7.11.13

Grant and Affiliation Information for Deletion analysis of protein kinase Calpha reveals a novel regulatory segment.

AFFILIATION: Department of Chemistry & Biochemistry Joslin Diabetes Center and Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02215, USA.

Country: JAPAN

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MEDLINETA: J Biochem

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