cAMP-dependent protein kinase A and the dynamics of epithelial cell surface domains: Moving membranes to keep in shape
Cyclic adenosine monophosphate (cAMP) and cAMP-dependent protein kinase A (PKA) are evolutionary conserved molecules with a well-established position in the complex network of signal transduction pathways. cAMP/PKA-mediated signaling pathways are implicated in many biological processes that cooperat...
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Published in | BioEssays Vol. 30; no. 2; pp. 146 - 155 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01.02.2008
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Subjects | |
Online Access | Get full text |
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Summary: | Cyclic adenosine monophosphate (cAMP) and cAMP-dependent protein kinase A (PKA) are evolutionary conserved molecules with a well-established position in the complex network of signal transduction pathways. cAMP/PKA-mediated signaling pathways are implicated in many biological processes that cooperate in organ development including the motility, survival, proliferation and differentiation of epithelial cells. Cell surface polarity, here defined as the anisotropic organisation of cellular membranes, is a critical parameter for most of these processes. Changes in the activity of cAMP/PKA elicit a variety of effects on intracellular membrane dynamics, including membrane sorting and trafficking. One of the most intriguing aspects of cAMP/PKA signaling is its evolutionary conserved abundance on the one hand and its precise spatial-temporal actions on the other. Here, we review recent developments with regard to the role of cAMP/PKA in the regulation of intracellular membrane trafficking in relation to the dynamics of epithelial surface domains. BioEssays 30:146-155, 2008. © 2008 Wiley Periodicals, Inc. |
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Bibliography: | http://dx.doi.org/10.1002/bies.20705 istex:BF9AD666B0A1B50C0C05B8E1B83AACFD213C0A95 ark:/67375/WNG-2RM50GCM-X ArticleID:BIES20705 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0265-9247 1521-1878 |
DOI: | 10.1002/bies.20705 |