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Dev Cell
2009 Jun 01;166:856-66. doi: 10.1016/j.devcel.2009.04.005.
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Metabolic control of oocyte apoptosis mediated by 14-3-3zeta-regulated dephosphorylation of caspase-2.
Nutt LK
,
Buchakjian MR
,
Gan E
,
Darbandi R
,
Yoon SY
,
Wu JQ
,
Miyamoto YJ
,
Gibbons JA
,
Gibbon JA
,
Andersen JL
,
Freel CD
,
Tang W
,
He C
,
Kurokawa M
,
Wang Y
,
Margolis SS
,
Fissore RA
,
Kornbluth S
.
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Xenopus oocyte death is partly controlled by the apoptotic initiator caspase-2 (C2). We reported previously that oocyte nutrient depletion activates C2 upstream of mitochondrial cytochrome c release. Conversely, nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. Although C2 dephosphorylation is responsive to metabolism, neither PP1 activity nor binding is metabolically regulated. Rather, release of 14-3-3zeta from C2 is controlled by metabolism and allows for C2 dephosphorylation. Accordingly, a C2 mutant unable to bind 14-3-3zeta is highly susceptible to dephosphorylation. Although this mechanism was initially established in Xenopus, we now demonstrate similar control of murine C2 by phosphorylation and 14-3-3 binding in mouse eggs. These findings provide an unexpected evolutionary link between 14-3-3 and metabolism in oocyte death.
Baliga,
The biochemical mechanism of caspase-2 activation.
2004, Pubmed
Baliga,
The biochemical mechanism of caspase-2 activation.
2004,
Pubmed
Bergeron,
Defects in regulation of apoptosis in caspase-2-deficient mice.
1998,
Pubmed
Cohen,
Protein phosphatase 1--targeted in many directions.
2002,
Pubmed
Danial,
Cell death: critical control points.
2004,
Pubmed
Danial,
BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis.
2003,
Pubmed
Datta,
14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation.
2000,
Pubmed
Duan,
RAIDD is a new 'death' adaptor molecule.
1997,
Pubmed
Egloff,
Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1.
1997,
Pubmed
Fissore,
Mechanisms underlying oocyte activation and postovulatory ageing.
2002,
Pubmed
Gasco,
Coincident inactivation of 14-3-3sigma and p16INK4a is an early event in vulval squamous neoplasia.
2002,
Pubmed
Hanoux,
Caspase-2 involvement during ionizing radiation-induced oocyte death in the mouse ovary.
2007,
Pubmed
Kurokawa,
Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization.
2007,
Pubmed
Majewski,
Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak.
2004,
Pubmed
Margolis,
PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation.
2003,
Pubmed
,
Xenbase
Margolis,
A role for PP1 in the Cdc2/Cyclin B-mediated positive feedback activation of Cdc25.
2006,
Pubmed
,
Xenbase
Nomura,
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax.
2003,
Pubmed
Nutt,
Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2.
2005,
Pubmed
,
Xenbase
Panaretakis,
Doxorubicin requires the sequential activation of caspase-2, protein kinase Cdelta, and c-Jun NH2-terminal kinase to induce apoptosis.
2005,
Pubmed
Pastorino,
Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis.
2002,
Pubmed
Rathmell,
Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival.
2003,
Pubmed
Read,
A novel Apaf-1-independent putative caspase-2 activation complex.
2002,
Pubmed
Rittinger,
Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding.
1999,
Pubmed
Robertson,
Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis.
2002,
Pubmed
Shenolikar,
Protein serine/threonine phosphatases--new avenues for cell regulation.
1994,
Pubmed
Smythe,
Systems for the study of nuclear assembly, DNA replication, and nuclear breakdown in Xenopus laevis egg extracts.
1991,
Pubmed
,
Xenbase
Sunayama,
JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3.
2005,
Pubmed
Tinel,
The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress.
2004,
Pubmed
Tsuruta,
JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.
2004,
Pubmed
Vietri,
Direct interaction between the catalytic subunit of Protein Phosphatase 1 and pRb.
2006,
Pubmed
Wakula,
Degeneracy and function of the ubiquitous RVXF motif that mediates binding to protein phosphatase-1.
2003,
Pubmed
Yaffe,
The structural basis for 14-3-3:phosphopeptide binding specificity.
1997,
Pubmed
Yang,
Structural basis for protein-protein interactions in the 14-3-3 protein family.
2006,
Pubmed
Zha,
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L).
1996,
Pubmed
Zhang,
Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.
1997,
Pubmed
Zhao,
Glycogen synthase kinase 3alpha and 3beta mediate a glucose-sensitive antiapoptotic signaling pathway to stabilize Mcl-1.
2007,
Pubmed
de Schepper,
Age-related changes of glucose-6-phosphate dehydrogenase activity in mouse oocytes.
1987,
Pubmed
