Mass spectrometric identification of Rab23 phosphorylation as a response to challenge by cytidine 3',5'-cyclic monophosphate in mouse brain

Biochemistry Group, Department of Biological Sciences, SOTEAS, Wallace Building, Swansea University, Singleton Park, Swansea SA2 8PP, UK.
Rapid Communications in Mass Spectrometry (Impact Factor: 2.25). 08/2007; 21(16):2685-92. DOI: 10.1002/rcm.3141
Source: PubMed


While the functions and mechanisms of action of adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP) are well established and are the basis of the action of a large number of successful pharmaceuticals, the role of a third naturally occurring cyclic nucleotide, cytidine 3',5'-cyclic monophosphate (cCMP), remains to be elucidated. Immobilized metal affinity chromatography (IMAC) was used to selectively extract proteins phosphorylated in mouse brain in response to challenge by cAMP, cGMP and cCMP, followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToFMS) and liquid chromatography/electrospray ionization tandem mass spectrometry (LC/ESI-MS/MS) of tryptic digests to identify Rab23 as the first protein reported to be phosphorylated only in response to cCMP.

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Available from: Robin Tuytten, Oct 10, 2015
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    • "Stability of cCMP against PDEs may result in sufficiently high cCMP concentrations that mediate physiological effects. cCMP-dependent phosphorylation was detected in mouse brain [25], and Rab23 was cCMP-dependently phosphorylated [26]. This observation could lead to identification of specific cCMP-dependent protein kinases which may, e.g. "
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