ArticleCell death & disease2012
Bcl-2 family member Bcl-G is not a proapoptotic protein.
Article in Cell death & disease, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- BCL-G: 20 years of research on a non-typical protein from the BCL-2 family.Cell death and differentiation · 2023Review
- Article
- Structural Details of BH3 Motifs and BH3-Mediated Interactions: an Updated Perspective.Frontiers in molecular biosciences · 2022Review
- Loss of Bcl-G, a Bcl-2 family member, augments the development of inflammation-associated colorectal cancer.Cell death and differentiation · 2020Article
- CMPK2 and BCL-G are associated with type 1 interferon-induced HIV restriction in humans.Science advances · 2018Article
- Article
- FocalScan: Scanning for altered genes in cancer based on coordinated DNA and RNA change.Nucleic acids research · 2016Article
- A potential molecular model for studying apoptosis enhanced by the interaction of BCL-G with JAB1 in swine.Oncotarget · 2016Article
- An RNA interference screen identifies new avenues for nephroprotection.Cell death and differentiation · 2016Article
- Functional and Structural Characterization of FAU Gene/Protein from Marine Sponge Suberites domuncula.Marine drugs · 2015Article
- MELK-a conserved kinase: functions, signaling, cancer, and controversy.Clinical and translational medicine · 2015Article
- Apolipoprotein L2 contains a BH3-like domain but it does not behave as a BH3-only protein.Cell death & disease · 2014Article
- Metabolic profiling of human CD4+ cells following treatment with methotrexate and anti-TNF-α infliximab.Cell cycle (Georgetown, Tex.) · 2013Article
- Bcl-G acquitted of murder!Cell death & disease · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three major subgroups of the Bcl-2 family, including the prosurvival Bcl-2-like proteins, the proapoptotic Bcl-2 homology (BH)3-only proteins and Bax/Bak proteins, regulate the mitochondrial apoptotic pathway. In addition, some outliers within the Bcl-2 family do not fit into these subgroups. One of them, Bcl-G, has a BH2 and a BH3 region, and was proposed to trigger apoptosis. To investigate the physiological role of Bcl-G, we have inactivated the gene in the mouse and generated monoclonal antibodies to determine its expression. Although two isoforms of Bcl-G exist in human, only one is found in mice. mBcl-G is expressed in a range of epithelial as well as in dendritic cells. Loss of Bcl-G did not appear to affect any of these cell types. mBcl-G only binds weakly to prosurvival members of the Bcl-2 family, and in a manner that is independent of its BH3 domain. To understand what the physiological role of Bcl-G might be, we searched for Bcl-G-binding partners through immunoprecipitation/mass spectroscopy and yeast-two-hybrid screening. Although we did not uncover any Bcl-2 family member in these screens, we found that Bcl-G interacts specifically with proteins of the transport particle protein complex. We conclude that Bcl-G most probably does not function in the classical stress-induced apoptosis pathway, but rather has a role in protein trafficking inside the cell.
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