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Information on EC 3.4.22.55 - caspase-2 and Organism(s) Mus musculus and UniProt Accession P29594
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3.4.22.55 caspase-2Specify your search results
Word Map
- 3.4.22.55
-
caspases
- bcl-2
- necrosis
- bid
-
proapoptotic
-
anti-apoptotic
- parp
- raidd
-
apoptosis-inducing
-
caspase-dependent
- z-vad-fmk
-
p53-induced
-
tunel
-
jurkat
-
polyadp-ribose
-
casps
-
mitochondria-mediated
-
non-apoptotic
-
pan-caspase
- apaf-1
- apoptosome
-
caspase-mediated
-
death-inducing
- cpp32
- fasl
- z-devd-fmk
-
executioner
- xiap
-
damage-induced
-
etoposide-induced
-
anti-fas
- prodomains
-
p53-dependent
-
trail-induced
-
executor
-
bh3-only
- ac-devd-cho
-
apoptogenic
-
trail-mediated
-
procaspase
- caspase-10
- chk1
-
beta-converting
-
mitochondria-dependent
- medicine
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for an Asp residue at P1, with Asp316 being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-/-
Synonyms
caspase-2, caspase 2, casp2, ich-1, casp-2, caspase-2l, nedd-2, caspase-2s, ajcasp, ich-1 protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C14.006
-
-
-
-
CASP-2
-
-
-
-
caspase 2
ICH-1 protease
-
-
-
-
ICH-1L/1S
-
-
-
-
caspase 2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
182372-14-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Bid + H2O
tBid + ?
-
active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization
-
-
?
MDM2 + H2O
MDM2 p60 + ?
-
active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53
-
-
?
tau protein + H2O
?
caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DELTAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease
-
-
?
BID + H2O
?
-
caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity
-
-
?
additional information
?
-
caspase-2 is a substrate for caspase-8 and caspase-3
-
-
?
additional information
?
-
-
phenotype of animals deficient in caspase-2: increased number of oocytes at birth, and oocytes are less susceptible to doxorubicin-induced apoptosis. B cells are partially resistant to death induction by granzyme B, accelerated apoptosis of facial motor neurons
-
-
?
additional information
?
-
-
caspase 2 is involved in ischemia-reperfusion-induced germ-cell-specific apoptosis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tau protein + H2O
?
caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DELTAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease
-
-
?
BID + H2O
?
-
caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity
-
-
?
Bid + H2O
tBid + ?
-
active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization
-
-
?
MDM2 + H2O
MDM2 p60 + ?
-
active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53
-
-
?
additional information
?
-
caspase-2 is a substrate for caspase-8 and caspase-3
-
-
?
additional information
?
-
-
phenotype of animals deficient in caspase-2: increased number of oocytes at birth, and oocytes are less susceptible to doxorubicin-induced apoptosis. B cells are partially resistant to death induction by granzyme B, accelerated apoptosis of facial motor neurons
-
-
?
additional information
?
-
-
caspase 2 is involved in ischemia-reperfusion-induced germ-cell-specific apoptosis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calcium/calmodulin regulated protein kinase II
phosphorylates caspase-2 at Ser-135
-
Cbzl-VDVAD-fluoromethylketone
-
caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RAIDD
adapter molecule, is required for caspase-2 activation after heat shock in splenocytes
-
ATM/ATR
-
caspase-2 is activated by ATM/ATR independently of p53 when Chk1 activity is repressed
-
RAIDD
-
in response to cellular stresses, processed PIDD-CC binds to RAIDD in the cytoplasm, which recruits and activates caspase-2, overview
-
additional information
heat shock, UV irradiation and anti-Fas treatment activate caspase-2
-
additional information
caspase-2 is activated by proximity-induced oligomerization and trans-cleavage in vitro. Caspase-2 activation is possibly also mediated by caspase-8 in the death-inducing signaling complex
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
caspase-2L activationis induced by ionizing radiation (0.5 Gy) in the 1 day postpartum. Caspase-2-dependent activation of the mitochondrial apoptotic pathway is one of the mechanisms involved in the genotoxic stress-induced depletion of the primordial follicle pool
-
shift of caspase 2 from the cytoplasm in the sham-operated testis to the mitochondria in the testis after torsion
caspase-2 activity transiently increases more than two-fold within 24 h following induction of differentiation
-
caspase-2 is required for apoptosis induced by cytoskeletal disruption. Caspase-2 mediates apoptosis via Piddosome, Bid and Bax activation, and cytochrome c release
-
embryonic fibroblasts deficient for both Bax and Bak indicate the contribution of both Bax and Bak in mediating cell death induced by resveratrol and the existence of Bax/Bak-independent cell death possibly through caspase-8- or caspase-2-mediated mitochondria-independent downstream caspase processing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
shift of caspase 2 from the cytoplasm in the sham-operated testis to the mitochondria in the testis after torsion
caspase-2 and p21 are localized to the nucleus during early differentiation
-
both precursor and processed caspase-2 localize to the cytoplasmic and nuclear compartments
-
shift of caspase 2 from the cytoplasm in the sham-operated testis to the mitochondria in the testis after torsion
-
the enzyme contains a classical nuclear localization signal at the C terminus of the prodomain which is recognized by the importin alpha/beta dimer
-
both precursor and processed caspase-2 localize to the cytoplasmic and nuclear compartments. Nuclear localization is strictly dependent on the presence of the prodomain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
physiological function
malfunction
cells lacking caspase-2 are protected from cell death induced by Staphylococcus aureus alpha-toxin
malfunction
down-regulation or inactivation of caspase-2 blocks amyloid beta-mediated effects on primary hippocampal cultures
malfunction
maturation, activation, and cytokine secretion are significantly impaired in Caspase-2 knockout cells infected with Brucella abortus strain RB51 or Salmonella typhimurium strain SL1344
malfunction
the loss of caspase-2 in mice results in an osteopenic phenotype associated with increased numbers of osteoclasts in vivo. Mitochondrial reactive oxygen species are significantly increased in caspase-deficient precursors after receptor activator of nuclear factor kappa-B ligand administration
malfunction
both pharmacological inhibition and shRNA-mediated knockdown of caspase-2 suppresses myogenic differentiation and dramatically impaired myotube formation
malfunction
caspase-2 deficiency leads to increased cellular stress largely because these mice fail to respond to oxidative stress by upregulating their antioxidant defense mechanism
malfunction
decreasing the levels of caspase-2 restores long-term memory in mice that have existing deficits
malfunction
loss of caspase-2 leads to an acceleration of tumor onset in the Emü-Myc mouse lymphoma model
metabolism
caspase-2 is a critical mediator in the activation of the RhoA/ROCK-II signaling pathway, leading to the collapse of dendritic spines. Inactive RhoA-GDP but not active RhoA-GTP forms a complex with caspase-2
metabolism
caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DETAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease
physiological function
Brucella abortus strain RB51- and S2308-induced BMDC cell death is regulated by caspase-2. The enzyme is required for naive T-lymphocyte proliferation following stimulation with RB51-infected bone marrow-derived dendritic cells
physiological function
caspase-2 is implicated in the regulation of cell death that is induced by metabolic imbalance, DNA damage, endoplasmic reticulum (ER) stress, mitotic catastrophe and others. Caspase-2 is implicated in the induction of cell death by pathogenic bacteria, such as Brucella, Staphylococcus aureus and Salmonella. Caspase-2 is controlling aging and cell death in response to DNA damage. The enzyme is also linked to cell death that is induced by aberrant mitosis in cancer cells that transiently arrest in prometaphase after cell fusion. Caspase 2 is crucial for oocyte apoptosis
physiological function
caspase-2 is involved in apoptosis, nuclear factor-kappaB regulation, and tumor suppression. Caspase-2 catalytic site Cys-320 and Ser-139 residues are required for caspase-2 to suppress tumorigenesis in nude mice
physiological function
caspase-2 modulates osteoclastogenesis through down-regulating oxidative stress
physiological function
caspase-2 plays a critical role in mediating the synaptic changes and memory alteration induced by amyloid beta in Alzheimer's disease
physiological function
in epithelial cells, caspase-2 is activated as an initiator caspase in a PIDDosome-independent manner to regulate pore-forming toxin-mediated cell death
physiological function
the enzyme is implicated in tumor suppression and plays a role in regulating the cellular response towards oxidative stress. Key cellular processes such as proliferation, aging, maintenance of genome surveillance and the redox system are affected by caspase-2 function
physiological function
caspase-2 acts as a tumor suppressor. Loss of caspase-2 leads to an acceleration of tumor onset in the EMy-Myc mouse lymphoma model
physiological function
caspase-2 is required for skeletal muscle differentiation and myogenesis. The role of caspase-2 is to regulate p21 induction at the onset of differentiation, which may regulate the myogenic program
physiological function
the enzyme is essential for mitochondrial oxidative stress-induced apoptosis
physiological function
the enzyme protects against oxidative stress in vivo
malfunction
-
Casp2-null animals develop normally, and thymocytes and neurons derived from them seem to undergo similar levels of apoptosis to those from wild-type littermates. Nevertheless, several subtle phenotypes are associated with the Casp2-knockout mice: Casp2-knockout females have a slight increase in the number of oocytes and Casp2/ oocytes show reduced apoptosis in response to treatment with doxorubicin. The neurons derived from Casp2-null mice are resistant to beta-amyloid-mediated death, which suggests a role for caspase 2 in neuronal death. Casp2-deficient mice also show signs of premature ageing, including accumulation of oxidative damage. Mouse embryonic fibroblasts from Casp2-deficient animals show a reduced or delayed apoptotic response to some cytotoxic drugs, have an aberrant DNA damage and cell cycle response and are readily transformed when they are challenged by oncogene expression.
malfunction
-
caspase-2 knockout mice do not develop early spontaneous tumors, but loss of caspase-2 in mice is associated with accelerated tumorigenesis driven by transgenic c-Myc on the mu-enhancer, thus caspase-2-deficient embryonic fibroblasts are more efficiently transformed than wild-type cells. Caspase-2-deficient mice have features consistent with accelerated ageing, phenotype, overview
physiological function
-
critical role of caspase-2 in mediating rough Brucella abortus induced macrophage cell death
physiological function
-
overview on the function of caspase-2 in cell death signaling
physiological function
-
role of caspase-2 in apoptosis, and caspase-2 may act as a tumor suppressor, mechanisms through which caspase-2 signals, e.g. involving PIDD, also known as LRDD or leucine-rich repeat and death domain-containing protein, caspase-2 pathways to apoptosis and cell cycle arrest, detailed overview. PIDD activation and more importantly caspase-2 activation is not always synonymous with induction of apoptosis, a threshold of caspase-2 activation must be reached before caspase-2-dependent apoptosis is engaged. Cleavage of Mdm2 is not the sole way caspase-2 can induce growth arrest
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CASP2_MOUSE
452
0
50661
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
caspase-2 is activated by dimerization, initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization. Dimerization results when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms
additional information
-
recruitment of caspase-2 to a higher molecular weight protein complex in cell extracts
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
additional information
-
DNA damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at S122 site within the prodomain leading to its cleavage and activation
phosphoprotein
calcium/calmodulin regulated protein kinase II phosphorylates caspase-2 at Ser-135
proteolytic modification
-
PIDD (p53-induced protein with a death domain [DD]), together with the bipartite adapter protein RAIDD (receptor-interacting protein-associated ICH-1/CED-3 homologous protein with a DD), is implicated in the activation of procaspase-2 in a high molecular weight complex called the PIDDosome during apoptosis induction after DNA damage. Processing of caspase-2 is readily detected in the absence of PIDDosome formation in primary lymphocytes
proteolytic modification
-
the initial activation of caspase 2 seems to be mediated by dimerization not processing, this generates a partially active enzyme that is further activated by autoprocessing (self cleavage). Additional processing, which is presumably mediated by active effector caspases (caspases 3 and 7) results in the generation of caspase 2 p19 and p12 subunits. Given that caspase 2 can be processed by caspases 3 and 7, and that loss or inhibition of these caspases or their upstream activators (caspase 9 and APAF1) leads to an inhibition of caspase 2 cleavage
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S139An
expression of mutant S139A leads to significantly enhanced growth rate of cells
K152A
-
mutant enzyme with strikingly altered caspase-2 localization. Whereas caspase-2 characteristically accumulates in the nucleus forming dots or filaments, the mutant enzyme is mostly localized outside and exclusively of the nucleus forming dot-like aggregates. K152A mutants can also kill transfected cells at comparable levels to the wild-type version
additional information
-
caspase prodomain-DELTA25 mutant is slightly less effective than wild-type caspase-2, inducing cell death of about 70% of transfected cells. Caspase prodomain-DELTA25 mutant cannot kill due to its impaired nuclear localization
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
caspase-2 enzyme activity in both Brucella abortus strain RB51- and S2308-infected bone marrow-derived dendritic cells is significantly up-regulated at 1 h, 4 h, and 24 h post infection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens, Mus musculus
van de Craen, M.; Vandenabeele, P.; Declercq, W.; van den Brande, I.; van Loo, G.; Molemans, F.; Schotte, P.; van Criekinge, W.; Beyaert, R.; Fiers, W.
Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus (P29594), Mus musculus C3H/An (P29594)
Kumar, S.; Kinoshita, M.; Noda, M.; Copeland, N.G.; Jenkins, N.A.
Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme
Genes Dev.
8
1613-1626
1994
Mus musculus (P29594), Mus musculus BALB/c (P29594)
Kumar, S.; Tomooka, Y.; Noda, M.
Identification of a set of genes with developmentally down-regulated expression in the mouse brain
Biochem. Biophys. Res. Commun.
185
1155-1161
1992
Mus musculus (P29594)
Colussi, P.A.; Harvey, N.L.; Shearwin-Whyatt, L.M.; Kumar, S.
Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
J. Biol. Chem.
273
26566-26570
1998
Mus musculus
Baliga, B.C.; Colussi, P.A.; Read, S.H.; Dias, M.M.; Jans, D.A.; Kumar, S.
Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
J. Biol. Chem.
278
4899-4905
2003
Mus musculus
Zheng, S.; Turner, T.T.; Lysiak, J.J.
Caspase 2 activity contributes to the initial wave of germ cell apoptosis during the first round of spermatogenesis
Biol. Reprod.
74
1026-1033
2006
Mus musculus (P29594), Mus musculus, Mus musculus C57BL/6 (P29594)
Bonzon, C.; Bouchier-Hayes, L.; Pagliari, L.J.; Green, D.R.; Newmeyer, D.D.
Caspase-2-induced apoptosis requires bid cleavage: a physiological role for bid in heat shock-induced death
Mol. Biol. Cell
17
2150-2157
2006
Mus musculus (P29594), Mus musculus, Xenopus laevis (Q9IB67)
Tu, S.; McStay, G.P.; Boucher, L.M.; Mak, T.; Beere, H.M.; Green, D.R.
In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
Nat. Cell Biol.
8
72-77
2006
Mus musculus (P29594)
Lysiak, J.J.; Zheng, S.; Woodson, R.; Turner, T.T.
Caspase-9-dependent pathway to murine germ cell apoptosis: mediation by oxidative stress, BAX, and caspase 2
Cell Tissue Res.
328
411-419
2007
Mus musculus
Hanoux, V.; Pairault, C.; Bakalska, M.; Habert, R.; Livera, G.
Caspase-2 involvement during ionizing radiation-induced oocyte death in the mouse ovary
Cell Death Differ.
14
671-681
2007
Mus musculus
Mohan, J.; Gandhi, A.A.; Bhavya, B.C.; Rashmi, R.; Karunagaran, D.; Indu, R.; Santhoshkumar, T.R.
Caspase-2 triggers Bax-Bak-dependent and -independent cell death in colon cancer cells treated with resveratrol
J. Biol. Chem.
281
17599-17611
2006
Homo sapiens, Mus musculus
Upton, J.P.; Austgen, K.; Nishino, M.; Coakley, K.M.; Hagen, A.; Han, D.; Papa, F.R.; Oakes, S.A.
Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress
Mol. Cell. Biol.
28
3943-3951
2008
Mus musculus
Ho, L.H.; Read, S.H.; Dorstyn, L.; Lambrusco, L.; Kumar, S.
Caspase-2 is required for cell death induced by cytoskeletal disruption
Oncogene
27
3393-3404
2008
Mus musculus
Krumschnabel, G.; Sohm, B.; Bock, F.; Manzl, C.; Villunger, A.
The enigma of caspase-2: The laymens view
Cell Death Differ.
16
195-207
2009
Homo sapiens, Mus musculus
Shi, M.; Vivian, C.J.; Lee, K.J.; Ge, C.; Morotomi-Yano, K.; Manzl, C.; Bock, F.; Sato, S.; Tomomori-Sato, C.; Zhu, R.; Haug, J.S.; Swanson, S.K.; Washburn, M.P.; Chen, D.J.; Chen, B.P.; Villunger, A.; Florens, L.; Du, C.
DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance
Cell
136
508-520
2009
Homo sapiens, Mus musculus
Narine, K.A.; Keuling, A.M.; Gombos, R.; Tron, V.A.; Andrew, S.E.; Young, L.C.
Defining the DNA mismatch repair-dependent apoptotic pathway in primary cells: evidence for p53-independence and involvement of centrosomal caspase 2
DNA Repair
9
161-168
2010
Mus musculus
Manzl, C.; Krumschnabel, G.; Bock, F.; Sohm, B.; Labi, V.; Baumgartner, F.; Logette, E.; Tschopp, J.; Villunger, A.
Caspase-2 activation in the absence of PIDDosome formation
J. Cell Biol.
185
291-303
2009
Mus musculus
Bouchier-Hayes, L.
The role of caspase-2 in stress-induced apoptosis
J. Cell. Mol. Med.
14
1212-1224
2010
Homo sapiens, Mus musculus
Kumar, S.
Caspase 2 in apoptosis, the DNA damage response and tumour suppression: enigma no more?
Nat. Rev. Cancer
9
897-903
2009
Mus musculus
Krumschnabel, G.; Manzl, C.; Villunger, A.
Caspase-2: killer, savior and safeguard-emerging versatile roles for an ill-defined caspase
Oncogene
28
3093-3096
2009
Mus musculus
Chen, F.; He, Y.
Caspase-2 mediated apoptotic and necrotic murine macrophage cell death induced by rough Brucella abortus
PLoS ONE
4
e6830
2009
Mus musculus
Vakifahmetoglu-Norberg, H.; Zhivotovsky, B.
The unpredictable caspase-2: what can it do?
Trends Cell Biol.
20
150-159
2010
Mus musculus
Bouchier-Hayes, L.; Green, D.R.
Caspase-2: the orphan caspase
Cell Death Differ.
19
51-57
2012
Homo sapiens, Mus musculus
Callaway, D.A.; Riquelme, M.A.; Sharma, R.; Lopez-Cruzan, M.; Herman, B.A.; Jiang, J.X.
Caspase-2 modulates osteoclastogenesis through down-regulating oxidative stress
Bone
76
40-48
2015
Mus musculus (P29594)
Imre, G.; Rajalingam, K.
Role for caspase-2 during pore-forming toxin-mediated apoptosis
Cell Cycle
11
3709-3710
2012
Mus musculus (P29594)
Ren, K.; Lu, J.; Porollo, A.; Du, C.
Tumor-suppressing function of caspase-2 requires catalytic site Cys-320 and site Ser-139 in mice
J. Biol. Chem.
287
14792-14802
2012
Mus musculus (P29594), Mus musculus
Fava, L.; Bock, F.; Geley, S.; Villunger, A.
Caspase-2 at a glance
J. Cell Sci.
125
5911-5915
2012
Mus musculus (P29594)
Pozueta, J.; Lefort, R.; Ribe, E.M.; Troy, C.M.; Arancio, O.; Shelanski, M.
Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
Nat. Commun.
4
1939
2013
Mus musculus (P29594), Mus musculus, Rattus norvegicus (P55215)
Olsson, M.; Forsberg, J.; Zhivotovsky, B.
Caspase-2: the reinvented enzyme
Oncogene
34
1877-1882
2015
Mus musculus (P29594), Mus musculus
Li, X.; He, Y.
Caspase-2-dependent dendritic cell death, maturation, and priming of T cells in response to Brucella abortus infection
PLoS ONE
7
e43512
2012
Mus musculus (P29594)
Boonstra, K.; Bloemberg, D.; Quadrilatero, J.
Caspase-2 is required for skeletal muscle differentiation and myogenesis
Biochim. Biophys. Acta Mol. Cell Res.
1865
95-104
2018
Mus musculus (P29594)
Lim, J.; Kim, H.K.; Kim, S.H.; Rhee, K.J.; Kim, Y.S.
Caspase-2 mediates triglyceride (TG)-induced macrophage cell death
BMB Rep.
50
510-515
2017
Mus musculus (P29594)
Peintner, L.; Dorstyn, L.; Kumar, S.; Aneichyk, T.; Villunger, A.; Manzl, C.
The tumor-modulatory effects of caspase-2 and Pidd1 do not require the scaffold protein Raidd
Cell Death Differ.
22
1803-1811
2015
Mus musculus (P29594), Mus musculus
Lopez-Cruzan, M.; Sharma, R.; Tiwari, M.; Karbach, S.; Holstein, D.; Martin, C.R.; Lechleiter, J.D.; Herman, B.
Caspase-2 resides in the mitochondria and mediates apoptosis directly from the mitochondrial compartment
Cell Death Dis.
2
16005
2016
Mus musculus (P29594)
Zhao, X.; Kotilinek, L.A.; Smith, B.; Hlynialuk, C.; Zahs, K.; Ramsden, M.; Cleary, J.; Ashe, K.H.
Caspase-2 cleavage of tau reversibly impairs memory
Nat. Med.
22
1268-1276
2016
Mus musculus (P29594), Homo sapiens (P42575), Homo sapiens
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