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The tail-anchoring domain of Bfl1 and HCCS1 targets mitochondrial membrane permeability to induce apoptosis

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dc.contributor.authorKo, Jae-Kyun-
dc.contributor.authorChoi, Kyoung-Han-
dc.contributor.authorPan, Zui-
dc.contributor.authorLin, Peihui-
dc.contributor.authorWeisleder, Noah-
dc.contributor.authorKim, Chul-Woo-
dc.contributor.authorMa, Jianjie-
dc.date.accessioned2009-10-01T04:53:38Z-
dc.date.available2009-10-01T04:53:38Z-
dc.date.issued2007-08-02-
dc.identifier.citationJ. Cell Sci. 120(Pt 16), 2912-2923en
dc.identifier.issn0021-9533 (Print)-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17666431-
dc.identifier.urihttp://hdl.handle.net/10371/10013-
dc.description.abstractMany Bcl2 family proteins target intracellular membranes by their C-terminal tail-anchor domain. Bfl1 is a bi-functional Bcl2 family protein with both anti- and pro-apoptotic activities and contains an amphipathic tail-anchoring peptide (ATAP; residues 147-175) with unique properties. Here we show that ATAP targets specifically to mitochondria, and induces caspase-dependent apoptosis that does not require Bax or Bak. Mutagenesis studies revealed that lysine residues flanking the ATAP sequence are involved in targeting of the peptide to the mitochondrial membrane, and charged residues that contribute to the amphipathic nature of ATAP are critical for its pro-apoptotic function. The ATAP sequence is present in another tumor suppressor gene, HCCS1, which contains an additional mitochondria-targeting signal (MTS) close to the ATAP. We propose that both ATAP and MTS could be used as therapeutic peptides to induce cell death in the treatment of cancer cells.en
dc.language.isoenen
dc.publisherCompany of Biologistsen
dc.subjectAmino Acid Sequenceen
dc.subject*Apoptosisen
dc.subjectBase Sequenceen
dc.subjectCell Line, Tumoren
dc.subjectConserved Sequenceen
dc.subjectLipid Bilayers/metabolismen
dc.subjectMembrane Potential, Mitochondrialen
dc.subjectMitochondrial Membranes/*metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectPeptides/chemistryen
dc.subjectPermeabilityen
dc.subjectProtein Sorting Signalsen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Transporten
dc.subjectProto-Oncogene Proteins c-bcl-2/*chemistry/genetics/*metabolismen
dc.subjectStructure-Activity Relationshipen
dc.subjectTumor Suppressor Proteins/*chemistry/genetics/*metabolismen
dc.subjectbcl-2 Homologous Antagonist-Killer Protein/metabolismen
dc.subjectbcl-2-Associated X Protein/metabolismen
dc.titleThe tail-anchoring domain of Bfl1 and HCCS1 targets mitochondrial membrane permeability to induce apoptosisen
dc.typeArticleen
dc.contributor.AlternativeAuthor고재균-
dc.contributor.AlternativeAuthor김철우-
dc.identifier.doi10.1242/jcs.006197-
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Pathology (병리학전공)Journal Papers (저널논문_병리학전공)
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