Competitive binding of protein kinase Calpha to membranes and Rho GTPases.

Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Research Abstract Details 

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Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Abstract Text:

Anthony C Cook,Cojen Ho,Jennifer L Kershner,Steve A Malinowski,Heath Moldveen,Brigid A Stagliano,Simon J Slater,

Previously, we have shown that protein kinase C (PKC) forms a direct high-affinity, isozyme-specific and membrane lipid-independent interaction with Rho GTPases [Slater, S. J., Seiz, J. L., Stagliano, B. A., and Stubbs, C. D. (2001) Biochemistry 40, 4437-4445]. Since the cellular activation of PKCalpha involves an initial translocation from cytosolic to membrane compartments, the present study investigates the interdependence between the direct protein-protein interaction of PKCalpha with the Rho GTPase, Cdc42, and the protein-lipid interactions of PKCalpha with membranes. It was hypothesized that the interaction of PKCalpha with membrane-bound Cdc42 would contribute to the overall membrane-binding affinity of the kinase by providing an additional anchor. However, it was found that the incorporation of isoprenylated Cdc42 into membranes resulted in an apparent decrease in the membrane-binding affinity of PKCalpha, whereas the association of PKCbetaI, PKCdelta, PKCepsilon, and PKCzeta was each unaffected. The presence of membrane-bound Cdc42 resulted in a rightward shift in both the PS- and Ca2+-concentration response curves for PKCalpha membrane association and for the ensuing activation, whereas the maximal levels of binding and activation attained at saturating PS and Ca2+ concentrations were in each case unaffected. Overall, these findings suggest that PKCalpha undergoes a isozyme-specific interaction with membrane-bound Cdc42 to form a PKCalpha-Cdc42 complex, which possesses a membrane-binding affinity that is reduced relative to that of the individual components due to competition between Cdc42 and PS/Ca2+ for binding to PKCalpha. Consistent with this, it was found that the interaction of PKCalpha with membrane-bound Cdc42 was accompanied by the physical dissociation of the PKCalpha-Cdc42 complex from membranes. Thus, the study provides a novel mechanism by which the membrane association and activation of PKCalpha and Cdc42 may be regulated by competing protein-protein and protein-lipid interactions.

Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Publishing Authors By Initials

AC Cook,C Ho,JL Kershner,SA Malinowski,H Moldveen,BA Stagliano,SJ Slater,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins research

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Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biochemistry

VOLUME: 45

Page Numbers: 14452-65

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 5

MONTH: Dec

YEAR: 2006

Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Keywords Mesh Terms:

KEYWORDS: rho GTP-Binding Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Competitive binding of protein kinase Calpha to membranes and Rho GTPases. Information

Substance Name: rho GTP-Binding Proteins

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Competitive binding of protein kinase Calpha to membranes and Rho GTPases.

AFFILIATION: Department of Pathology and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.

Country: United States

AGENCY: United States NIAAA

GRANT: AA010990

ACRONYM: AA

MEDLINETA: Biochemistry

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