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Cover Picture: Sphingosine Kinase Interacting Protein is an A‐Kinase Anchoring Protein Specific for Type I cAMP‐Dependent Protein Kinase (ChemBioChem 7/2010)
Author(s) -
Kovanich Duangnapa,
van der Heyden Marcel A. G.,
Aye Thin Thin,
van Veen Toon A. B.,
Heck Albert J. R.,
Scholten Arjen
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201090025
Subject(s) - protein kinase a , protein subunit , protein data bank (rcsb pdb) , chemistry , kinase , biochemistry , protein kinase domain , microbiology and biotechnology , biology , gene , mutant
The cover picture shows a collage of crystal structures of the regulatory subunit of cAMP‐dependent protein kinase (PKA‐R). At the bottom, the dimeric N‐terminal dimerization domain (13–62) of PKA‐RIα in complex with the D‐AKAP2 anchoring domain (green, PDB ID: 3IM4). On top, two units of PKA‐RIα (92–380, 1RGS, red and blue) with four molecules of bound cAMP (black). A chemical proteomics approach using immobilized synthetic cAMP analogues (8‐AHA‐cAMP and 8AHA‐2′‐OMe‐cAMP, top right) was amended to show that SPHKAP is the first mammalian PKA‐RI‐specific AKAP. Isotope‐labeled dimethylation (MS spectrum) was used for quantitation. SPHKAP was found to be highly expressed in human heart. Specific amino acids at specific locations in the anchoring domain of SPHKAP obey all the postulated rules to drive the observed PKA‐RI specificity. For more information, see the paper by A. Scholten et al. on p. 963 ff. (The background was generated from an image of the heart of a 64‐year‐old male taken from Wikipedia.)