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.

scholarly journals Plasma Membrane Na+/H+Exchanger Isoforms (NHE-1, −2, and −3) Are Differentially Responsive to Second Messenger Agonists of the Protein Kinase A and C Pathways

1995 ◽  
Vol 270 (49) ◽  
pp. 29209-29216 ◽  
Author(s):  
Ramani A. Kandasamy ◽  
Frank H. Yu ◽  
Robert Harris ◽  
Annie Boucher ◽  
John W. Hanrahan ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Second Messenger ◽  
Kinase A

cAMP increases liver Na+-taurocholate cotransport by translocating transporter to plasma membranes

1997 ◽  
Vol 273 (4) ◽  
pp. G842-G848 ◽  
Author(s):  
Sunil Mukhopadhayay ◽  
M. Ananthanarayanan ◽  
Bruno Stieger ◽  
Peter J. Meier ◽  
Frederick J. Suchy ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Fusion Protein ◽  
Protein Kinase A ◽  
Plasma Membranes ◽  
Membrane Vesicles ◽  
Rat Hepatocytes ◽  
Plasma Membrane Vesicles ◽  
Short Term ◽  
Kinase A

Adenosine 3′,5′-cyclic monophosphate (cAMP), acting via protein kinase A, increases transport maximum of Na+-taurocholate cotransport within 15 min in hepatocytes (S. Grüne, L. R. Engelking, and M. S. Anwer. J. Biol. Chem. 268: 17734–17741, 1993); the mechanism of this short-term stimulation was investigated. Cycloheximide inhibited neither basal nor cAMP-induced increases in taurocholate uptake in rat hepatocytes, indicating that cAMP does not stimulate transporter synthesis. Studies in plasma membrane vesicles showed that taurocholate uptake was not stimulated by the catalytic subunit of protein kinase A but was higher when hepatocytes were pretreated with cAMP. Immunoblot studies with anti-fusion protein antibodies to the cloned Na+-taurocholate cotransport polypeptide (Ntcp) showed that pretreatment of hepatocytes with cAMP increased Ntcp content in plasma membranes but not in homogenates. Ntcp was detected in microsomes, endosomes, and Golgi fractions, and cAMP pretreatment resulted in a decrease only in endosomal Ntcp content. It is proposed that cAMP increases transport maximum of Na+-taurocholate cotransport, at least in part, by translocating Ntcp from endosomes to plasma membranes.

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.

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

The control of blood platelets by cAMP signalling

2014 ◽  
Vol 42 (2) ◽  
pp. 289-294 ◽  
Author(s):  
Zaher Raslan ◽  
Khalid M. Naseem
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Platelet Activation ◽  
Blood Platelets ◽  
Blood Platelet ◽  
Platelet Inhibition ◽  
Signalling Pathway ◽  
Current Understanding ◽  
Camp Signalling ◽  
Kinase A

Blood platelet activation must be tightly regulated to ensure a balance between haemostasis and thrombosis. The cAMP signalling pathway is the most powerful endogenous regulator of blood platelet activation. PKA (protein kinase A), the foremost effector of cAMP signalling in platelets, phosphorylates a number of proteins that are thought to modulate multiple aspects of platelet activation. In the present mini-review, we outline our current understanding of cAMP-mediated platelet inhibition and discuss some of the issues that require clarification.

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