Literature DB >> 33291826

The Mysteries around the BCL-2 Family Member BOK.

Raed Shalaby1, Hector Flores-Romero1, Ana J García-Sáez1.   

Abstract

BOK is an evolutionarily conserved BCL-2 family member that resembles the apoptotic effectors BAK and BAX in sequence and structure. Based on these similarities, BOK has traditionally been classified as a BAX-like pro-apoptotic protein. However, the mechanism of action and cellular functions of BOK remains controversial. While some studies propose that BOK could replace BAK and BAX to elicit apoptosis, others attribute to this protein an indirect way of apoptosis regulation. Adding to the debate, BOK has been associated with a plethora of non-apoptotic functions that makes this protein unpredictable when dictating cell fate. Here, we compile the current knowledge and open questions about this paradoxical protein with a special focus on its structural features as the key aspect to understand BOK biological functions.

Entities:  

Keywords:  BCL-2 family; BOK; MOMP; apoptosis

Mesh:

Substances:

Year:  2020        PMID: 33291826      PMCID: PMC7762061          DOI: 10.3390/biom10121638

Source DB:  PubMed          Journal:  Biomolecules        ISSN: 2218-273X


  89 in total

1.  Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function.

Authors:  Lin Chen; Simon N Willis; Andrew Wei; Brian J Smith; Jamie I Fletcher; Mark G Hinds; Peter M Colman; Catherine L Day; Jerry M Adams; David C S Huang
Journal:  Mol Cell       Date:  2005-02-04       Impact factor: 17.970

2.  Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis.

Authors:  Estefanía Lucendo; Mónica Sancho; Fabio Lolicato; Matti Javanainen; Waldemar Kulig; Diego Leiva; Gerard Duart; Vicente Andreu-Fernández; Ismael Mingarro; Mar Orzáez
Journal:  Proc Natl Acad Sci U S A       Date:  2020-10-22       Impact factor: 11.205

Review 3.  Mitochondria as multifaceted regulators of cell death.

Authors:  Florian J Bock; Stephen W G Tait
Journal:  Nat Rev Mol Cell Biol       Date:  2019-10-21       Impact factor: 94.444

4.  Lipidic pore formation by the concerted action of proapoptotic BAX and tBID.

Authors:  Oihana Terrones; Bruno Antonsson; Hirohito Yamaguchi; Hong-Gang Wang; Jihua Liu; Ray M Lee; Andreas Herrmann; Gorka Basañez
Journal:  J Biol Chem       Date:  2004-05-11       Impact factor: 5.157

Review 5.  Structural biology of the Bcl-2 family and its mimicry by viral proteins.

Authors:  M Kvansakul; M G Hinds
Journal:  Cell Death Dis       Date:  2013-11-07       Impact factor: 8.469

6.  Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction.

Authors:  A Y Robin; K Krishna Kumar; D Westphal; A Z Wardak; G V Thompson; G Dewson; P M Colman; P E Czabotar
Journal:  Cell Death Dis       Date:  2015-07-09       Impact factor: 8.469

7.  Negative Regulation of BOK Expression by Recruitment of TRIM28 to Regulatory Elements in Its 3' Untranslated Region.

Authors:  Yuniel Fernandez-Marrero; Daniel Bachmann; Emanuel Lauber; Thomas Kaufmann
Journal:  iScience       Date:  2018-11-10

8.  BCL-2 family protein BOK is a positive regulator of uridine metabolism in mammals.

Authors:  Rahul Srivastava; Zhipeng Cao; Christina Nedeva; Samara Naim; Daniel Bachmann; Tatiana Rabachini; Lahiru Gangoda; Sanjay Shahi; Jason Glab; Joseph Menassa; Laura Osellame; Tao Nelson; Yuniel Fernandez-Marrero; Fiona Brown; Andrew Wei; Francine Ke; Lorraine O'Reilly; Marcel Doerflinger; Cody Allison; Andrew Kueh; Rob Ramsay; Brian J Smith; Suresh Mathivanan; Thomas Kaufmann; Hamsa Puthalakath
Journal:  Proc Natl Acad Sci U S A       Date:  2019-07-16       Impact factor: 11.205

9.  BID-induced structural changes in BAK promote apoptosis.

Authors:  Tudor Moldoveanu; Christy R Grace; Fabien Llambi; Amanda Nourse; Patrick Fitzgerald; Kalle Gehring; Richard W Kriwacki; Douglas R Green
Journal:  Nat Struct Mol Biol       Date:  2013-04-21       Impact factor: 15.369

10.  An interconnected hierarchical model of cell death regulation by the BCL-2 family.

Authors:  Hui-Chen Chen; Masayuki Kanai; Akane Inoue-Yamauchi; Ho-Chou Tu; Yafen Huang; Decheng Ren; Hyungjin Kim; Shugaku Takeda; Denis E Reyna; Po M Chan; Yogesh Tengarai Ganesan; Chung-Ping Liao; Evripidis Gavathiotis; James J Hsieh; Emily H Cheng
Journal:  Nat Cell Biol       Date:  2015-09-07       Impact factor: 28.824

View more
  3 in total

1.  Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptor.

Authors:  Laura M Szczesniak; Caden G Bonzerato; Jacqualyn J Schulman; Alaji Bah; Richard J H Wojcikiewicz
Journal:  Biochem Biophys Res Commun       Date:  2021-03-24       Impact factor: 3.575

2.  BCL-2-family protein tBID can act as a BAX-like effector of apoptosis.

Authors:  Hector Flores-Romero; Lisa Hohorst; Malina John; Marie-Christine Albert; Louise E King; Laura Beckmann; Tamas Szabo; Vanessa Hertlein; Xu Luo; Andreas Villunger; Lukas P Frenzel; Hamid Kashkar; Ana J Garcia-Saez
Journal:  EMBO J       Date:  2021-12-21       Impact factor: 11.598

3.  Identification of the Bok Interactome Using Proximity Labeling.

Authors:  Laura M Szczesniak; Caden G Bonzerato; Richard J H Wojcikiewicz
Journal:  Front Cell Dev Biol       Date:  2021-05-31
  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.