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 |
| Item ID: | 56408 |
| Date Deposited: | 07 Aug 2008 |
| Last Modified: | 11 Jun 2013 01:45 |
| Contributors: | Campbell, Linda E. (Author) Proud, Christopher G. (Author) |
| Date: | 2 January 2002 |
| Status: | Published |
| URI: | http://eprints.soton.ac.uk/id/eprint/56408 |
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