Bcl-2-related survival proteins

Schwartz, Pamela S.; Hockenbery, David M.

doi:10.1038/sj.cdd.4401982

Cell Death Differ

2006

DOI: 10.1038/sj.cdd.4401982

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Bcl-2-related survival proteins

Pamela S. Schwartz

David M. Hockenbery

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Cited by 19 publications

(24 citation statements)

References 80 publications

(70 reference statements)

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“…The members of the Bcl-2 family of proteins are essential regulators of cell survival and apoptosis in metazoans. [1][2][3][4] The members of this Bcl-2 family share one to four Bcl-2 homology (BH) domains. The prosurvival proteins, such as Bcl-2 and Bcl-X L , are characterized by the presence of BH1-BH4 domains and act to maintain the integrity of mitochondria to prevent the release of cytochrome c. 1,2 The members of the proapoptotic Bax subfamily (Bax, Bak and Bok) contain BH1-BH3 domains and are required for mitochondrial outer membrane (MOM) permeabilization.…”

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confidence: 99%

“…MA-dependent subcellular localization is critical for the correct function of both prosurvival and proapoptotic Bcl-2 homologues. [1][2][3][4] In a comprehensive study, Kaufmann et al 5 described the molecular basis for the differential intracellular localization of Bcl-2 and Bcl-X L . They found that multiple positively charged residues flanking the MA of Bcl-X L that are absent in Bcl-2 appear to determine the localization of Bcl-X L to specific membrane compartments.…”

mentioning

confidence: 99%

“…[1][2][3][4] The members of this Bcl-2 family share one to four Bcl-2 homology (BH) domains. The prosurvival proteins, such as Bcl-2 and Bcl-X L , are characterized by the presence of BH1-BH4 domains and act to maintain the integrity of mitochondria to prevent the release of cytochrome c. 1,2 The members of the proapoptotic Bax subfamily (Bax, Bak and Bok) contain BH1-BH3 domains and are required for mitochondrial outer membrane (MOM) permeabilization. 1,3 The BH3-only proteins such as Bid, Bad, Bik, Bim, Noxa and Puma respond to various death stimuli and induce cell death in a Bax/Bakdependent manner or by antagonizing the prosurvival Bcl-2 proteins.…”

mentioning

confidence: 99%

“…1,3 The BH3-only proteins such as Bid, Bad, Bik, Bim, Noxa and Puma respond to various death stimuli and induce cell death in a Bax/Bakdependent manner or by antagonizing the prosurvival Bcl-2 proteins. 1,2 Most Bcl-2 family members contain a C-terminal hydrophobic membrane anchor (MA). [1][2][3][4] The MA mediates the intracellular localization of these proteins to membranes of the mitochondria, ER and nuclear envelope.…”

mentioning

confidence: 99%

“…1,2 Most Bcl-2 family members contain a C-terminal hydrophobic membrane anchor (MA). [1][2][3][4] The MA mediates the intracellular localization of these proteins to membranes of the mitochondria, ER and nuclear envelope. MA-dependent subcellular localization is critical for the correct function of both prosurvival and proapoptotic Bcl-2 homologues.…”

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confidence: 99%

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Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY

2007

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The Bcl-2-family of proteins localize to intracellular membranes via a C-terminal hydrophobic membrane anchor (MA) domain, to exert their antiapoptotic or proapoptotic functions. In Drosophila, both Bcl-2 family members, DEBCL and BUFFY, contain an MA. In DEBCL the MA is necessary for the localization of protein to mitochondria and for its proapoptotic activity. BUFFY is highly similar to DEBCL but its localization and function are not clearly defined. Here, we report on comparative analysis of BUFFY and DEBCL to decipher the molecular basis for their subcellular localization. We show that these two proteins localize to distinct intracellular membranes, DEBCL predominantly to mitochondria and BUFFY to endoplasmic reticula (ER). Our results suggest that the MA-flanking residues in DEBCL, homologous to Bcl-X L , are required for the targeting of DEBCL to mitochondria. The C-terminal positively charged residues present in DEBCL are absent in BUFFY, which allows for its localization to ER. The MA in both proteins is required for the correct targeting and proapoptotic activities of these proteins. Interestingly, a functional nuclear localization signal was identified in the N-terminal region of BUFFY and in the absence of the MA, BUFFY accumulated in the nucleus. The functional implications of these findings are discussed. The members of the Bcl-2 family of proteins are essential regulators of cell survival and apoptosis in metazoans. [1][2][3][4] The members of this Bcl-2 family share one to four Bcl-2 homology (BH) domains. The prosurvival proteins, such as Bcl-2 and Bcl-X L , are characterized by the presence of BH1-BH4 domains and act to maintain the integrity of mitochondria to prevent the release of cytochrome c. 1,2 The members of the proapoptotic Bax subfamily (Bax, Bak and Bok) contain BH1-BH3 domains and are required for mitochondrial outer membrane (MOM) permeabilization. 1,3 The BH3-only proteins such as Bid, Bad, Bik, Bim, Noxa and Puma respond to various death stimuli and induce cell death in a Bax/Bakdependent manner or by antagonizing the prosurvival Bcl-2 proteins. 1,2Most Bcl-2 family members contain a C-terminal hydrophobic membrane anchor (MA). [1][2][3][4] The MA mediates the intracellular localization of these proteins to membranes of the mitochondria, ER and nuclear envelope. MA-dependent subcellular localization is critical for the correct function of both prosurvival and proapoptotic Bcl-2 homologues. [1][2][3][4] In a comprehensive study, Kaufmann et al. 5 described the molecular basis for the differential intracellular localization of Bcl-2 and Bcl-X L . They found that multiple positively charged residues flanking the MA of Bcl-X L that are absent in Bcl-2 appear to determine the localization of Bcl-X L to specific membrane compartments. The authors suggest that in the absence of such a strong positive charge, Bcl-2 is able to localize to other membranes as well as mitochondria. 5 There are two Bcl-2 family members in Drosophila, BUFFY and DEBCL, both of which are closely related to mammal...

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confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY

2007

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Mitochondria in neurodegenerative disorders: regulation of the redox state and death signaling leading to neuronal death and survival

Naoi¹,

Maruyama

Yi³

et al. 2009

J Neural Transm

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In Parkinson's disease, impaired function of mitochondrial complex I is involved in selective degeneration of dopamine neurons in the substantia nigra. Mitochondria are now considered to play an active role in neuronal death process through activating "intrinsic" apoptotic signaling, in addition to production of reactive oxygen species. This paper presents our recent findings on new functions of mitochondria in regulation of their redox state and function through reversible "S-glutathionylation", a mixed disulfide binding between sulfhydryl groups of GSH and protein cysteine in complex I subunits. Type A monoamine oxidase (MAO-A) localized at the mitochondrial outer membrane is a binding site of neurotoxins leading to apoptosis. Rasagiline and (-)deprenyl, type B MAO inhibitors of propagylamine-derivatives, bind to MAO-A to protect neuronal cells against apoptosis through induction of pro-survival Bcl-2 and neurotrophic factors. This review discusses the new role of mitochondria in regulation of neuronal cell death of neurodegenerative disorders.

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Betulinic Acid Induces Bax/Bak-Independent Cytochrome c Release in Human Nasopharyngeal Carcinoma Cells

Liu

Luo

2012

Molecules and Cells

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Bcl-2-related survival proteins

Cited by 19 publications

References 80 publications

Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY

Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY

Mitochondria in neurodegenerative disorders: regulation of the redox state and death signaling leading to neuronal death and survival

Betulinic Acid Induces Bax/Bak-Independent Cytochrome c Release in Human Nasopharyngeal Carcinoma Cells

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