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Dynamic cAMP fluctuations that are restricted to a sub-plasma-membrane domain strengthen endothelial barrier integrity. Phosphodiesterases (PDEs) localize within this domain where they limit cAMP diffusion into the bulk cytosolic compartment; however, the molecular identity of PDEs responsible for endothelial cell membrane cAMP compartmentation remain poorly understood. Our present findings reveal that the D4 splice variant of the PDE4 phosphodiesterase family - PDE4D4 - is expressed in pulmonary microvascular endothelial cells, and is found in plasma membrane fractions. PDE4D4 interacts with
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JCS ePress
online publication date 11 Dec 2007
doi: 10.1242/jcs.011692
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jcs.011692v1
121/1/110
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Research Article
Spectrin-anchored phosphodiesterase 4D4 restricts cAMP from disrupting microtubules and inducing endothelial cell gap formation
* Author for correspondence (e-mail: tstevens{at}jaguar1.usouthal.edu)
II spectrin within this membrane domain. Although constitutive PDE4D4 activity limits cAMP access to the bulk cytosol, inhibiting its activity permits cAMP to access a cytosolic domain that is rich in microtubules, where it promotes protein kinase A (PKA) phosphorylation of tau at Ser214. Such phosphorylation reorganizes microtubules and induces interendothelial cell gap formation. Thus, spectrin-anchored PDE4D4 shapes the physiological response to cAMP by directing it to barrier-enhancing effectors while limiting PKA-mediated microtubule reorganization.
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N. Prasain, M. Alexeyev, R. Balczon, and T. Stevens
Soluble adenylyl cyclase-dependent microtubule disassembly reveals a novel mechanism of endothelial cell retraction
Am J Physiol Lung Cell Mol Physiol,
July 1, 2009;
297(1):
L73 - L83.
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B. Zhu, L. Zhang, M. Alexeyev, D. F. Alvarez, S. J. Strada, and T. Stevens
Type 5 phosphodiesterase expression is a critical determinant of the endothelial cell angiogenic phenotype
Am J Physiol Lung Cell Mol Physiol,
February 1, 2009;
296(2):
L220 - L228.
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© The Company of Biologists Ltd 2007