Caspase substrates
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Caspases are a family of cysteinyl proteases that regulate apoptosis and other biological processes. Caspase-3 is considered the central executioner member of this family with a wide range of substrates.
14p viwyoming2711 16-12-2020 9 1 Download
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Anovel caspase-like activity, which is directly regulatedwith cell proliferation is a candidate to regulate the abundance of the cyclin-dependent kinase inhibitor, p27 KIP1 , in human lymphoid cells.This activity, whichwe termKIPase activity, can also cleave a subset of caspase substrates.Here we demonstrate thatKIPase is anovel enzymedistinct fromany of the previously characterized human caspases.
8p dell39 03-04-2013 38 2 Download
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We have previously shown that lovastatin induces apoptosis in spontane-ously immortalized rat brain neuroblasts. Focal adhesion proteins and pro-tein kinase Cd(PKCd) have been implicated in the regulation of apoptosis. We found that lovastatin exposure induced focal adhesion kinase, Crk-asso-ciated substrate (p130 Cas ), PKCdcleavage and caspase-3 activation in a con-centration-dependent manner. Lovastatin effects were fully prevented by mevalonate.
13p dell39 27-03-2013 38 2 Download
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Many protein substrates of caspases are cleaved at noncanonical sites in comparison to the recognition motifs reported for the three caspase sub-groups. To provide insight into the specificity and aid in the design of drugs to control cell death, crystal structures of caspase-7 were determined in complexes with six peptide analogs (Ac-DMQD-Cho, Ac-DQMD-Cho, Ac-DNLD-Cho, Ac-IEPD-Cho, Ac-ESMD-Cho, Ac-WEHD-Cho) that span the major recognition motifs of the three subgroups.
14p media19 04-03-2013 37 3 Download
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DYRK1A is a member of the dual-specificity tyrosine-phosphorylation-reg-ulated protein kinase family and is implicated in Down’s syndrome. Here, we identify the cysteine aspartyl protease caspase9, a critical component of the intrinsic apoptotic pathway, as a substrate of DYRK1A. Depletion of DYRK1A from human cells by short interfering RNA inhibits the basal phosphorylation of caspase9 at an inhibitory site, Thr125.
13p vinaphone15 28-02-2013 34 1 Download