scholarly journals Distinct Protein Kinase A Anchoring Proteins Direct Prostaglandin E2Modulation of Toll-like Receptor Signaling in Alveolar Macrophages

2011 ◽  
Vol 286 (11) ◽  
pp. 8875-8883 ◽  
Author(s):  
Sang-Hoon Kim ◽  
Carlos Henrique Serezani ◽  
Katsuhide Okunishi ◽  
Zbigniew Zaslona ◽  
David M. Aronoff ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Alveolar Macrophages ◽  
Receptor Signaling ◽  
Toll Like Receptor ◽  
Anchoring Proteins ◽  
Kinase A

A-kinase-anchoring proteins and cytoskeletal signalling events

2003 ◽  
Vol 31 (1) ◽  
pp. 87-89 ◽  
Author(s):  
J.D. Scott
Keyword(s):  
Protein Kinase ◽  
Molecular Mass ◽  
Protein Kinase A ◽  
Protein Kinases ◽  
Recent Progress ◽  
Membrane Receptors ◽  
Anchoring Proteins ◽  
Syndrome Protein ◽  
Kinase A

Targeting of protein kinases and phosphatases to the cytoskeleton enhances the regulation of many signalling events. Cytoskeletal signalling complexes facilitate this process by optimizing the relay of messages from membrane receptors to specific sites on the actin cytoskeleton. These signals influence fundamental cell properties such as shape, movement and division. Targeting of the cAMP-dependent kinase (protein kinase A) and other enzymes to this compartment is achieved through interaction with A-kinase-anchoring proteins (AKAPs). The present paper discusses recent progress on dissecting the biological role of WAVE1 (Wiskott–Alrich syndrome protein family verprolin homology protein 1), an AKAP that assembles a cytoskeletal transduction complex in response to signals that emanate from the low-molecular-mass GTPase, Rac.

Characterization of RIIβ and D-AKAP1 in differentiated adipocytes

2002 ◽  
Vol 282 (1) ◽  
pp. C205-C212 ◽  
Author(s):  
Archana Chaudhry ◽  
Chen Zhang ◽  
James G. Granneman
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Immunocytochemical Analysis ◽  
Subcellular Compartments ◽  
Anchoring Proteins ◽  
Mitotracker Red ◽  
Kinase A

A-kinase anchoring proteins (AKAPs) have been proposed to regulate cAMP-dependent signaling in the cell by targeting RII subunits of protein kinase A (PKA) to specific subcellular compartments. RIIβ is the predominant PKA subtype in adipose tissue. In gel overlay assays of C3H/10T1/2 adipocytes and adipose tissue, RIIβ bound to several proteins including a prominent 132-kDa band, which was strongly induced upon differentiation of C3H/10T1/2 cells into adipocytes. Immunoblotting and nuclease protection analysis of C3H/10T1/2 cellular extracts identified this band as D-AKAP1/S-AKAP84, a putative AKAP. Immunocytochemical analysis of C3H/10T1/2 adipocytes revealed that most of D-AKAP1/S-AKAP84, but not RIIβ, was colocalized with a mitochondrial-selective dye, MitoTracker red. These findings were further confirmed in studies where D-AKAP1/ S-AKAP84, but not RIIβ, were localized in purified mitochondria made from C3H/10T1/2 adipocytes. Moreover, D-AKAP1, which is upregulated after differentiation, did not recruit RIIβto membrane fractions enriched in mitochondria. These results demonstrate that D-AKAP1/S-AKAP84 does not interact with PKA in differentiated C3H/10T1/2 adipocytes under the conditions tested.

scholarly journals Protein Kinase A Anchoring Proteins Are Required for Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells

1999 ◽  
Vol 274 (8) ◽  
pp. 4934-4938 ◽  
Author(s):  
Enno Klussmann ◽  
Kenan Maric ◽  
Burkhard Wiesner ◽  
Michael Beyermann ◽  
Walter Rosenthal
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Cell Membranes ◽  
Principal Cells ◽  
Aquaporin 2 ◽  
Anchoring Proteins ◽  
Kinase A

scholarly journals Gravin Orchestrates Protein Kinase A and  2-Adrenergic Receptor Signaling Critical for Synaptic Plasticity and Memory

2012 ◽  
Vol 32 (50) ◽  
pp. 18137-18149 ◽  
Author(s):  
R. Havekes ◽  
D. A. Canton ◽  
A. J. Park ◽  
T. Huang ◽  
T. Nie ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Receptor Signaling ◽  
Kinase A

Restricted diffusion of a freely diffusible second messenger: mechanisms underlying compartmentalized cAMP signalling

2006 ◽  
Vol 34 (4) ◽  
pp. 495-497 ◽  
Author(s):  
M. Zaccolo ◽  
G. Di Benedetto ◽  
V. Lissandron ◽  
L. Mancuso ◽  
A. Terrin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Second Messenger ◽  
Restricted Diffusion ◽  
Selective Activation ◽  
Camp Signalling ◽  
Anchoring Proteins ◽  
Structural Mechanisms ◽  
Kinase A

It is becoming increasingly evident that the freely diffusible second messenger cAMP can transduce specific responses by localized signalling. The machinery that underpins compartmentalized cAMP signalling is only now becoming appreciated. Adenylate cyclases, the enzymes that synthesize cAMP, are localized at discrete parts of the plasma membrane, and phosphodiesterases, the enzymes that degrade cAMP, can be targeted to selected subcellular compartments. A-kinase-anchoring proteins then serve to anchor PKA (protein kinase A) close to specific targets, resulting in selective activation. The specific activation of such individual subsets of PKA requires that cAMP is made available in discrete compartments. In this presentation, the molecular and structural mechanisms responsible for compartmentalized PKA signalling and restricted diffusion of cAMP will be discussed.

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