For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
0
views
90
references
 Top references
cited by
0
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      505
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Bcl-B: an “unknown” protein of the Bcl-2 family

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Bcl-B is a poorly understood protein of the Bcl-2 family that is highly expressed in many healthy tissues and tumor types. Bcl-B is considered an antiapoptotic protein, but many reports have revealed its contradictory roles in different cancer types. In this mini-review, we elucidate the functions of Bcl-B in normal conditions and various pathologies, its regulation of programmed cell death, its oncogene/oncosuppressor activity in tumorigenesis, its impact on drug-acquired resistance, and possible approaches to inhibit Bcl-B.

          Related collections

          Most cited references90

          • Record: found
          • Abstract: not found
          • Article: not found

          The Hallmarks of Cancer

          Douglas Hanahan, Robert Weinberg (2000)
          Article 0 comments Cited 2231 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Self-eating and self-killing: crosstalk between autophagy and apoptosis.

            M Chiara Maiuri, Einat Zalckvar, Adi Kimchi … (2007)
            The functional relationship between apoptosis ('self-killing') and autophagy ('self-eating') is complex in the sense that, under certain circumstances, autophagy constitutes a stress adaptation that avoids cell death (and suppresses apoptosis), whereas in other cellular settings, it constitutes an alternative cell-death pathway. Autophagy and apoptosis may be triggered by common upstream signals, and sometimes this results in combined autophagy and apoptosis; in other instances, the cell switches between the two responses in a mutually exclusive manner. On a molecular level, this means that the apoptotic and autophagic response machineries share common pathways that either link or polarize the cellular responses.
            Article 0 comments Cited 445 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy.

              Sophie Pattingre, Amina T Tassa, Xueping Qu … (2005)
              Apoptosis and autophagy are both tightly regulated biological processes that play a central role in tissue homeostasis, development, and disease. The anti-apoptotic protein, Bcl-2, interacts with the evolutionarily conserved autophagy protein, Beclin 1. However, little is known about the functional significance of this interaction. Here, we show that wild-type Bcl-2 antiapoptotic proteins, but not Beclin 1 binding defective mutants of Bcl-2, inhibit Beclin 1-dependent autophagy in yeast and mammalian cells and that cardiac Bcl-2 transgenic expression inhibits autophagy in mouse heart muscle. Furthermore, Beclin 1 mutants that cannot bind to Bcl-2 induce more autophagy than wild-type Beclin 1 and, unlike wild-type Beclin 1, promote cell death. Thus, Bcl-2 not only functions as an antiapoptotic protein, but also as an antiautophagy protein via its inhibitory interaction with Beclin 1. This antiautophagy function of Bcl-2 may help maintain autophagy at levels that are compatible with cell survival, rather than cell death.
              Article 0 comments Cited 327 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                G. S. Kopeina: lirroster@gmail.com
                B. Zhivotovsky: boris.zhivotovsky@ki.se
                Journal
                Journal ID (nlm-ta): Biol Direct
                Journal ID (iso-abbrev): Biol Direct
                Title: Biology Direct
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1745-6150
                Publication date (Electronic): 30 October 2023
                Publication date PMC-release: 30 October 2023
                Publication date Collection: 2023
                Volume: 18
                Electronic Location Identifier: 69
                Affiliations
                [1 ]GRID grid.4886.2, ISNI 0000 0001 2192 9124, Engelhardt Institute of Molecular Biology, , Russian Academy of Sciences, ; Moscow, 119991 Russia
                [2 ]Faculty of Medicine, MV Lomonosov Moscow State University, ( https://ror.org/010pmpe69) Moscow, 119991 Russia
                [3 ]Division of Toxicology, Institute of Environmental Medicine, Karolinska Institute, ( https://ror.org/056d84691) Box 210, Stockholm, 17177 Sweden
                Article
                Publisher ID: 431
                DOI: 10.1186/s13062-023-00431-4
                PMC ID: 10614328
                PubMed ID: 37899453
                SO-VID: 2cdc20e1-5b9b-40db-ab9b-8936b431d82d
                Copyright © © The Author(s) 2023
                License:

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

                History
                Date received : 19 October 2023
                Date accepted : 23 October 2023
                Funding
                Funded by: Karolinska Institute
                Open Access :

                Open access funding provided by Karolinska Institute.

                Categories
                Subject: Review
                Custom metadata
                issue-copyright-statement © BioMed Central Ltd., part of Springer Nature 2023

                ScienceOpen disciplines: Life sciences
                Keywords: bcl-b/bcl-2l10,bcl-2 family proteins,carcinogenesis,programmed cell death,oogenesis,embryogenesis
                Data availability:
                ScienceOpen disciplines: Life sciences
                Keywords: bcl-b/bcl-2l10, bcl-2 family proteins, carcinogenesis, programmed cell death, oogenesis, embryogenesis

                Comments

                Comment on this article