Functional implications of assigned, assumed and assembled PKC structures

2014 ◽  
Vol 42 (1) ◽  
pp. 35-41 ◽  
Author(s):  
Mark Linch ◽  
Philippe Riou ◽  
Jeroen Claus ◽  
Angus J. Cameron ◽  
Julien de Naurois ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Family Members ◽  
Pharmacological Intervention ◽  
Signalling Pathways ◽  
Membrane Targeting ◽  
Domain Structures ◽  
Kinase C ◽  
Functional Implications ◽  
Pkc Protein Kinase C

The empirical derivation of PKC (protein kinase C) domain structures and those modelled by homology or imputed from protein behaviour have been extraordinarily valuable both in the elucidation of PKC pathway mechanisms and in the general lessons that extrapolate to other signalling pathways. For PKC family members, there are many domain/subdomain structures and models, covering all of the known domains, variably present in this family of protein serine/threonine kinases (C1, C2, PB1, HR1, kinase domains). In addition to these structures, there are a limited number of complexes defined, including the structure of the PKCε V3–14-3-3 complex. In the context of structure-driven insights into PKC pathways, there are several broadly applicable principles and mechanisms relevant to the operation of and intervention in signalling pathways. These principles have an impact in unexpected ways, from the regulation of membrane targeting, through strategies for pharmacological intervention, to biomarkers.

scholarly journals Protein kinase C in cellular transformation: a valid target for therapy?

2014 ◽  
Vol 42 (6) ◽  
pp. 1556-1562 ◽  
Author(s):  
Anuradha Tarafdar ◽  
Alison M. Michie
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
B Cell ◽  
Critical Role ◽  
Prognostic Significance ◽  
Family Members ◽  
Cellular Transformation ◽  
Signalling Pathways ◽  
Kinase C ◽  
Pkc Isoforms

The protein kinase C (PKC) family of serine/threonine protein kinases share structural homology, while exhibiting substantial functional diversity. PKC isoforms are ubiquitously expressed in tissues which makes it difficult to define roles for individual isoforms, with complexity compounded by the finding that PKC isoforms can co-operate with or antagonize other PKC family members. A number of studies suggest the involvement of PKC family members in regulating leukaemic cell survival and proliferation. Chronic lymphocytic leukaemia (CLL), the most common leukaemia in the Western world, exhibits dysregulated expression of PKC isoforms, with recent reports indicating that PKCβ and δ play a critical role in B-cell development, due to their ability to link the B-cell receptor (BCR) with downstream signalling pathways. Given the prognostic significance of the BCR in CLL, inhibition of these BCR/PKC-mediated signalling pathways is of therapeutic relevance. The present review discusses the emerging role of PKC isoforms in the pathophysiology of CLL and assesses approaches that have been undertaken to modulate PKC activity.

scholarly journals Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.

1994 ◽  
Vol 269 (51) ◽  
pp. 32358-32367
Author(s):  
A Toker ◽  
M Meyer ◽  
K K Reddy ◽  
J R Falck ◽  
R Aneja ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Family Members ◽  
The Novel ◽  
Kinase C

scholarly journals Membrane Targeting and Cytoplasmic Sequestration in the Spatiotemporal Localization of Human Protein Kinase C α

2000 ◽  
Vol 275 (8) ◽  
pp. 6014-6021 ◽  
Author(s):  
Alice Vallentin ◽  
Corinne Prévostel ◽  
Teddy Fauquier ◽  
Xavier Bonnefont ◽  
Dominique Joubert
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Protein ◽  
Membrane Targeting ◽  
Kinase C ◽  
Human Protein Kinase ◽  
Spatiotemporal Localization

Lifespan regulation of conventional protein kinase C isotypes

2007 ◽  
Vol 35 (5) ◽  
pp. 1043-1045 ◽  
Author(s):  
D. Carmena ◽  
A. Sardini
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Second Messengers ◽  
Therapeutic Strategies ◽  
Kinase C ◽  
Signalling Network ◽  
Pkc Protein Kinase C ◽  
Lifespan Regulation

Plasma membrane translocation, following allosteric binding of second messengers, initiates the signal transduction process mediated by cPKC [conventional PKC (protein kinase C)] isotypes. Mechanisms regulating the lifespan of the active enzyme such as its phosphorylation, internalization, dephosphorylation and degradation are key elements of the signalling network. The understanding of such mechanisms is essential for the design of therapeutic strategies targeting PKC isoenzymes.

Regulation of exocytosis by protein kinase C

2005 ◽  
Vol 33 (6) ◽  
pp. 1341-1344 ◽  
Author(s):  
A. Morgan ◽  
R.D. Burgoyne ◽  
J.W. Barclay ◽  
T.J. Craig ◽  
G.R. Prescott ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Types ◽  
Neuroendocrine Cells ◽  
Protein Targets ◽  
Site Specific ◽  
Regulated Exocytosis ◽  
Kinase C ◽  
Pkc Protein Kinase C

PKC (protein kinase C) has been known for many years to modulate regulated exocytosis in a wide variety of cell types. In neurons and neuroendocrine cells, PKC regulates several different stages of the exocytotic process, suggesting that these multiple actions of PKC are mediated by phosphorylation of distinct protein targets. In recent years, a variety of exocytotic proteins have been identified as PKC substrates, the best characterized of which are SNAP-25 (25 kDa synaptosome-associated protein) and Munc18. In the present study, we review recent evidence suggesting that site-specific phosphorylation of SNAP-25 and Munc18 by PKC regulates distinct stages of exocytosis.

Sign in / Sign up

Export Citation Format

Share Document