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ProteomicsAurora kinase B-dependent phosphorylation regulates caspase-2 activity and function
Mitotic catastrophe (MC) is an important mechanism to remove cells that become polyploid or aneuploid, as an oncosuppressive mechanism. Previous studies have demonstrated that the activation and catalytic function of caspase-2 is a key step in MC, to trigger apoptosis and/or cell cycle arrest of suc...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-09 | PXD017866 | Pride
Aurorka kinase Caspase 2 Phosphorylation 
ProteomicsCaspase-2 protects against ferroptotic cell death
To identify proteins that interact with caspase-2 that could potentially explain its ability to regulate ferroptosis, we performed an unbiased BioID proteomics screen.
ORGANISM(S): Homo sapiens (Human) 
2024-03-06 | PXD041339 | Pride
Caspase-2  ferroptosis  mutant-p53  chaperone mediated autophagy 
ProteomicsCaspase-2 is a condensate-mediated deubiquitinase in protein quality control
When cells encounter proteome stresses, caspase-2 accumulates in a ubiquitin-rich condensate, which functions as a deubiquitinase to cleave the overloaded ubiquitinated proteins.
ORGANISM(S): Homo Sapiens 
PXD041964 |
ProteomicsAge-related proteomic profiling of livers from Caspase-2 deficient mice
Caspase-2 function in liver homeostasis is influenced by its important role in mitotic catastrophe to prevent survival and accumulation of aneuploid and polyploid cells. While loss of caspase-2 promotes hepatocyte polyploidy, it is unclear how this influences liver homeostasis with ageing. To addres...
ORGANISM(S): Mus musculus (Mouse) 
2025-11-20 | PXD063938 | Pride
Mus musculus Proteolytic mutation Liver Ageing Caspase-2 Polyploidy 
GenomicsCaspase-2 and the PIDDosome do not control aneuploidy in hepatocellular carcinoma
Caspase-2 and the PIDDosome do not control aneuploidy in hepatocellular carcinoma
PRJEB35930 | ENA
GenomicsCaspase-2 and the PIDDosome do not control aneuploidy in hepatocellular carcinoma
Caspase-2 and the PIDDosome do not control aneuploidy in hepatocellular carcinoma
PRJEB35931 | ENA
ProteomicsHuman recombinant caspase 2-3-7
COFRADIC identification of human recombinant caspase-2, -3, -7 cleavage sites
ORGANISM(S): Homo sapiens (Human) 
2012-08-15 | PRD000557 | Pride
ProteomicsAn integrated chemoproteomic and screening platform identifies a functional and ligandable non-catalytic cysteine in caspase-2
Caspases are a highly conserved family of cysteine-aspartyl proteases known for their essential roles in regulating apoptosis, inflammation, cell differentiation and proliferation. Complementary to genetic approaches, small molecule inhibitors have emerged as useful tools for modulating caspase acti...
ORGANISM(S): Homo sapiens (Human) 
2025-01-14 | PXD051381 | Pride
Caspase-2 Jurkats Isotop Eclipse 
ProteomicsAn integrated chemoproteomic and screening platform identifies a functional and ligandable non-catalytic cysteine in caspase-2
Caspases are a highly conserved family of cysteine-aspartyl proteases known for their essential roles in regulating apoptosis, inflammation, cell differentiation and proliferation. Complementary to genetic approaches, small molecule inhibitors have emerged as useful tools for modulating caspase acti...
ORGANISM(S): Homo sapiens (Human) 
2025-01-14 | PXD042362 | Pride
Faims Isotop-abpp Ligandable Caspase-2 
GenomicsCaspase-2 is essential for proliferation and self-renewal of nucleophosmin-mutated acute myeloid leukemia
Caspase-2 is essential for proliferation and self-renewal of nucleophosmin-mutated acute myeloid leukemia
PRJNA1049463 | ENA
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