Caspase-3-mediated Cleavage of Akt: Involvement of Non-consensus Sites and Influence of Phosphorylation.
From: Department of Obstetrics and Gynaecology, University of Ottawa, Ottawa, Canada.
FEBS letters
- Publish Date: Jun 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 16
- Pages: 2883-8
- Medium: Print
- Language: English
- Citation (JAMA): Jahani-Asl Arezu, Basak Ajoy, Tsang Benjamin K, et al. Caspase-3-mediated Cleavage of Akt: Involvement of Non-consensus Sites and Influence of Phosphorylation.. FEBS Lett. Jun 2007;581:2883-8
Abstract
Here, we show for the first time that Akt1 is cleaved in vitro at the caspase-3 consensus site DQDD(456) downward arrow SM. Our data suggest QEEE(116) downward arrow E(117) downward arrow MD, EEMD(119) downward arrow, TPPD(453) downward arrow QD and DAKE(398) downward arrow IM as novel non-consensus caspase-3 cleavage sites. More importantly, we demonstrate that phosphorylation of Akt1 modulates its cleavage in a site-specific manner: Resistance to cleavage at site DAKE(398) (within the kinase domain) in response to phosphorylation suggests a possible mechanism by which the anti-apoptotic role of Akt1 is regulated. Our result is important in biological models which rely on Akt1 for cell survival.
Mesh Headings (Keywords): Amino Acid Motifs, Binding Sites, Caspase 3, Consensus Sequence, Humans, Phosphorylation, Protein Kinases, Protein Processing, Post-Translational, Proto-Oncogene Proteins c-akt, Sequence Analysis, Protein
Check for Full Text / PubMed Unique Identifier (PMID): 17544405
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