Differing substrate specificities of members of the DYRK family of arginine-directed protein kinases


Campbell, Linda E. and Proud, Christopher G. (2002) Differing substrate specificities of members of the DYRK family of arginine-directed protein kinases. FEBS Letters, 510, (1-2), 31-36. (doi:10.1016/S0014-5793(01)03221-5).

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Description/Abstract

The mammalian DYRK (dual specificity tyrosine phosphorylated and regulated kinase) family of protein kinases comprises a number of related, but poorly understood enzymes. DYRK1A is nuclear while DYRKs 2 and 3 are cytoplasmic. We recently showed that DYRK2 phosphorylates the translation initiation factor eIF2B at Ser539 in its ε-subunit and thereby ‘primes’ its phosphorylation by glycogen synthase kinase-3. Here we have used peptides based on the sequence around Ser539 to help define the specificity of DYRK2/3 in comparison with DYRK1A. These kinases require an arginine N-terminal to the target residue for efficient substrate phosphorylation. This cannot be replaced even by lysine. A peptide with arginine at −2 is phosphorylated much less well by all three kinases than one with arginine at −3. Replacement of the +1 proline by alanine almost completely eliminates substrate phosphorylation, but valine here does allow phosphorylation especially by DYRK2. This study reveals both similarities and differences in the specificities of these arginine-dependent protein kinases.

Item Type: Article
ISSNs: 0014-5793 (print)
Related URLs:
Keywords: protein kinase, DYRK, proline, minbrain, initiation factor, eIF
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56408
Date Deposited: 07 Aug 2008
Last Modified: 27 Mar 2014 18:39
URI: http://eprints.soton.ac.uk/id/eprint/56408

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