(Q45953801)

18 December 2017

title

Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy. (English)

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18 December 2017

2

Alexandra C Newton

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18 December 2017

author name string

Daniel R Dries

series ordinal

1

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18 December 2017

language of work or name

English

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publication date

10 January 2008

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18 December 2017

Journal of Biological Chemistry

published in

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18 December 2017

volume

283

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18 December 2017

issue

12

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18 December 2017

page(s)

7885-7893

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18 December 2017

Protein kinase C: structure, function, and regulation

cites work

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Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions

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A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production

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Increased membrane affinity of the C1 domain of protein kinase Cdelta compensates for the lack of involvement of its C2 domain in membrane recruitment

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Membrane binding kinetics of protein kinase C betaII mediated by the C2 domain

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Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling

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A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C

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Signaling and subcellular targeting by membrane-binding domains

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

21 January 2018

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Interaction of protein kinase C with phosphatidylserine. 1. Cooperativity in lipid binding

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

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Supplementation of the phosphatidyl-L-serine requirement of protein kinase C with nonactivating phospholipids

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Lipid structure and not membrane structure is the major determinant in the regulation of protein kinase C by phosphatidylserine.

21 January 2018

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

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Protein kinase C regulatory domains: the art of decoding many different signals in membranes

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C1 domains exposed: from diacylglycerol binding to protein-protein interactions

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Competitive inhibition by diacylglycerol of specific phorbol ester binding

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Control of astrocyte Ca(2+) oscillations and waves by oscillating translocation and activation of protein kinase C.

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Protein kinase C (PKC) family in cancer progression

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Protein kinase C and other diacylglycerol effectors in cancer

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Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cdelta

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Membrane-protein interactions in cell signaling and membrane trafficking

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Contribution of the C1A and C1B Domains to the Membrane Interaction of Protein Kinase C

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Mechanism of the apparent cooperativity in the interaction of protein kinase C with phosphatidylserine.

21 January 2018

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Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin

21 January 2018

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Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains

21 January 2018

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Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation

21 January 2018

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How proteins adapt to a membrane-water interface

21 January 2018

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Visualization of transient encounter complexes in protein-protein association.

21 January 2018

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Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M709943200

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18 December 2017

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18 December 2017