We are analyzing https://link.springer.com/article/10.1007/s10495-007-0746-4.

Title:
Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes | Apoptosis
Description:
Permeabilization of the outer mitochondrial membrane is the point of no return in most programmed cell deaths. This critical step is mainly regulated by the various protein-protein and protein-membrane interactions of the Bcl-2 family proteins. The two main models for regulation of mitochondrial outer membrane permeabilization, direct activation and displacement do not account for all of the experimental data and both largely neglect the importance of the membrane. We propose the embedding together model to emphasize the critical importance of Bcl-2 family protein interactions with and within membranes. The embedding together model proposes that both pro- and anti-apoptotic Bcl-2 family proteins engage in similar dynamic interactions that are governed by membrane dependent conformational changes and culminate in either aborted or productive membrane permeabilization depending on the final oligomeric state of pro-apoptotic Bax and/or Bak.
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Keywords {🔍}

article, google, scholar, pubmed, cas, bax, cell, apoptosis, bcl, biol, mitochondrial, membrane, chem, death, bak, family, protein, proapoptotic, mol, bid, proteins, cancer, mitochondria, science, bclxl, interaction, activation, conformational, bhonly, cytochrome, permeabilization, release, genes, dev, usa, nat, privacy, cookies, change, leber, lin, cheng, tbid, proc, natl, acad, sci, molecular, tan, mcl,

Topics {✒️}

cytomegalovirus-encoded mitochondria-localized inhibitor bcl-xl-bak peptide complex c-terminal membrane anchor bid-induced open conformer membrane-targeted death ligand bid-induced conformational change phospho-ser 15-p53 translocates inhibiting vaccinia-induced apoptosis bak-mediated mitochondrial apoptosis bh3-ligand regulates access hydrocarbon-stapled bh3 helix protein-membrane interactions outer mitochondrial membrane bcl-2 family proteins article leber membrane dependent conformational inhibiting bak auto-oligomerization privacy choices/manage cookies reversible conformational change bak-mcl1 complex ligand-induced activation bak-mediated apoptosis membrane surface triggers prosurvival bcl-2 proteins eugenol-induced apoptosis cytokine-induced apoptosis leu ji final oligomeric state membrane-bound bcl-2 activate mitochondrial apoptosis author correspondence cheng eh lipidic pore formation high potency activation clusterin inhibits apoptosis mitochondrial cristae reorganization similar dynamic interactions programmed cell deaths related subjects soluble monomeric protein pro-apoptotic bax proapoptotic protein bak european economic area walensky ld chipuk je del gaizo moore form supramolecular openings posttranslational n-myristoylation willis sn dna damage response

Questions {❓}

Lazebnik Y (2002) Can a biologist fix a radio?

Schema {🗺️}

WebPage:
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         headline:Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
         description:Permeabilization of the outer mitochondrial membrane is the point of no return in most programmed cell deaths. This critical step is mainly regulated by the various protein-protein and protein-membrane interactions of the Bcl-2 family proteins. The two main models for regulation of mitochondrial outer membrane permeabilization, direct activation and displacement do not account for all of the experimental data and both largely neglect the importance of the membrane. We propose the embedding together model to emphasize the critical importance of Bcl-2 family protein interactions with and within membranes. The embedding together model proposes that both pro- and anti-apoptotic Bcl-2 family proteins engage in similar dynamic interactions that are governed by membrane dependent conformational changes and culminate in either aborted or productive membrane permeabilization depending on the final oligomeric state of pro-apoptotic Bax and/or Bak.
         datePublished:2007-02-15T00:00:00Z
         dateModified:2007-02-15T00:00:00Z
         pageStart:897
         pageEnd:911
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            Bax
            MOMP
            Mitochondrial permeabilization
            Membrane proteins
            Cancer Research
            Cell Biology
            Oncology
            Biochemistry
            general
            Virology
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ScholarlyArticle:
      headline:Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
      description:Permeabilization of the outer mitochondrial membrane is the point of no return in most programmed cell deaths. This critical step is mainly regulated by the various protein-protein and protein-membrane interactions of the Bcl-2 family proteins. The two main models for regulation of mitochondrial outer membrane permeabilization, direct activation and displacement do not account for all of the experimental data and both largely neglect the importance of the membrane. We propose the embedding together model to emphasize the critical importance of Bcl-2 family protein interactions with and within membranes. The embedding together model proposes that both pro- and anti-apoptotic Bcl-2 family proteins engage in similar dynamic interactions that are governed by membrane dependent conformational changes and culminate in either aborted or productive membrane permeabilization depending on the final oligomeric state of pro-apoptotic Bax and/or Bak.
      datePublished:2007-02-15T00:00:00Z
      dateModified:2007-02-15T00:00:00Z
      pageStart:897
      pageEnd:911
      sameAs:https://doi.org/10.1007/s10495-007-0746-4
      keywords:
         Bcl-2
         Bax
         MOMP
         Mitochondrial permeabilization
         Membrane proteins
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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         name:Departments of Biochemistry and Biomedical Sciences and Medicine, McMaster University, Hamilton, Canada
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