Premium
Mass spectrometric identification of Rab23 phosphorylation as a response to challenge by cytidine 3′,5′‐cyclic monophosphate in mouse brain
Author(s) -
Bond A. Elizabeth,
Dudley Edward,
Tuytten Robin,
Lemière Filip,
Smith Christopher J.,
Esmans Eddy L.,
Newton Russell P.
Publication year - 2007
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.3141
Subject(s) - chemistry , cyclic guanosine monophosphate , cyclic adenosine monophosphate , cytidine , guanosine , mass spectrometry , phosphorylation , chromatography , electrospray ionization , tandem mass spectrometry , cyclic nucleotide , nucleotide , adenosine , biochemistry , enzyme , receptor , organic chemistry , nitric oxide , gene
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. Copyright © 2007 John Wiley & Sons, Ltd.