Literature DB >> 34616865

Yes, MAM!

Robert E Means1, Samuel G Katz1.   

Abstract

Regulation of cell life and death by members of the BCL-2 family of proteins occurs at the mitochondria. Large portions of the mitochondria's outer membrane are found in tight approximation with the endoplasmic reticulum (ER), known as mitochondria-associated membranes (MAMs) or mitochondria-ER contact sites (MERCs). We recently reported that BOK is present within MAMs where it regulates Ca2+ transfer from the ER to the mitochondria, appropriate MAM components and MERC structure, and apoptosis.
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Entities:  

Keywords:  BCL-2; BOK; MAM; MERC; apoptosis; calcium

Year:  2021        PMID： 34616865      PMCID： PMC8489963          DOI： 10.1080/23723556.2021.1919473

Source DB:  PubMed          Journal:  Mol Cell Oncol        ISSN： 2372-3556


  10 in total

Review 1.  Non-apoptotic functions of BCL-2 family proteins.

Authors:  Atan Gross; Samuel G Katz
Journal:  Cell Death Differ       Date:  2017-02-24       Impact factor: 15.828

2.  BIRD-2, a BH4-domain-targeting peptide of Bcl-2, provokes Bax/Bak-independent cell death in B-cell cancers through mitochondrial Ca2+-dependent mPTP opening.

Authors:  Martijn Kerkhofs; Rita La Rovere; Kirsten Welkenhuysen; Ann Janssens; Peter Vandenberghe; Muniswamy Madesh; Jan B Parys; Geert Bultynck
Journal:  Cell Calcium       Date:  2021-01-12       Impact factor: 6.817

Review 3.  The deadly landscape of pro-apoptotic BCL-2 proteins in the outer mitochondrial membrane.

Authors:  Mark P A Luna-Vargas; Jerry E Chipuk
Journal:  FEBS J       Date:  2016-01-06       Impact factor: 5.542

4.  Direct Activation of BAX by BTSA1 Overcomes Apoptosis Resistance in Acute Myeloid Leukemia.

Authors:  Denis E Reyna; Thomas P Garner; Andrea Lopez; Felix Kopp; Gaurav S Choudhary; Ashwin Sridharan; Swathi-Rao Narayanagari; Kelly Mitchell; Baoxia Dong; Boris A Bartholdy; Loren D Walensky; Amit Verma; Ulrich Steidl; Evripidis Gavathiotis
Journal:  Cancer Cell       Date:  2017-10-09       Impact factor: 31.743

Review 5.  ER-mitochondria interactions: Both strength and weakness within cancer cells.

Authors:  Mabrouka Doghman-Bouguerra; Enzo Lalli
Journal:  Biochim Biophys Acta Mol Cell Res       Date:  2019-01-19       Impact factor: 4.739

6.  Bok regulates mitochondrial fusion and morphology.

Authors:  Jacqualyn J Schulman; Laura M Szczesniak; Eric N Bunker; Heather A Nelson; Michael W Roe; Larry E Wagner; David I Yule; Richard J H Wojcikiewicz
Journal:  Cell Death Differ       Date:  2019-04-11       Impact factor: 15.828

7.  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

8.  Bok Is Not Pro-Apoptotic But Suppresses Poly ADP-Ribose Polymerase-Dependent Cell Death Pathways and Protects against Excitotoxic and Seizure-Induced Neuronal Injury.

Authors:  Beatrice D'Orsi; Tobias Engel; Shona Pfeiffer; Saheli Nandi; Thomas Kaufmann; David C Henshall; Jochen H M Prehn
Journal:  J Neurosci       Date:  2016-04-20       Impact factor: 6.167

9.  BOK controls apoptosis by Ca2+ transfer through ER-mitochondrial contact sites.

Authors:  Marcos A Carpio; Robert E Means; Allison L Brill; Alva Sainz; Barbara E Ehrlich; Samuel G Katz
Journal:  Cell Rep       Date:  2021-03-09       Impact factor: 9.423
  10 in total

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