Roles of ionic residues of the C1 domain in protein kinase C-alpha activation and the origin of phosphatidylserine specificity. (Q40849607)

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1 November 2019

title

Roles of ionic residues of the C1 domain in protein kinase C-alpha activation and the origin of phosphatidylserine specificity (English)

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1 November 2019

1

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1 November 2019

Robert V. Stahelin

series ordinal

2

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1 November 2019

author name string

Cho W

series ordinal

3

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1 November 2019

language of work or name

English

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publication date

11 October 2000

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Journal of Biological Chemistry

1 November 2019

published in

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1 November 2019

volume

276

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1 November 2019

issue

6

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1 November 2019

page(s)

4218-4226

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Protein kinase C: structure, function, and regulation

1 November 2019

cites work

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Regulation of protein kinase C.

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Regulation of protein kinase C betaII by its C2 domain

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Mutagenesis of the C2 domain of protein kinase C-alpha. Differential roles of Ca2+ ligands and membrane binding residues

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Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+

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Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine

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Phorbol ester binding to protein kinase C requires a cysteine-rich zinc-finger-like sequence

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Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester

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Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers

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Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules.

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Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells

21 January 2018

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Protein kinase Calpha contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities.

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Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation

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Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals

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Interplay of C1 and C2 domains of protein kinase C-alpha in its membrane binding and activation

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Differential membrane-binding and activation mechanisms of protein kinase C-alpha and -epsilon

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Phosphoinositide-specific phospholipase C-delta 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate

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Association of protein kinase C with phospholipid monolayers: two-stage irreversible binding

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Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors

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The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain

21 January 2018

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The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner

21 January 2018

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