Journal
MOLECULAR BIOSYSTEMS
Volume 1, Issue 4, Pages 325-331Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b511267b
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Funding
- NCI NIH HHS [R24CA88317] Funding Source: Medline
- NIEHS NIH HHS [ES06676] Funding Source: Medline
- NIGMS NIH HHS [GM66170] Funding Source: Medline
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Exchange protein directly activated by cAMP (Epac) is a newly discovered cAMP receptor that mediates the intracellular cAMP actions in addition to the classic cAMP-dependent protein kinase system, In this study, we show that Epac interacts directly with tubulin, co-purifies with cellular microtubules, and co-localizes with the mitotic spindle assembly. Association with microtubules suppresses Epac-mediated Rapl activation, while the binding of Epac promotes microtubule formation. These results demonstrate that Epac plays an important role in connecting the microtubule cytoskeleton network and intracellular cAMP-signalling.
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