VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel?

作者: Svetlana Rajkumar Maurya , Radhakrishnan Mahalakshmi

DOI: 10.1111/FEBS.13637

关键词:

摘要: The voltage-dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such required for cellular metabolism. elaborate interplay between mitochondria apoptotic pathway supports a role VDACs major regulator cell death. Although VDAC-1 has an established in apoptosis homeostasis, VDAC-2 been controversial. In humans, is best known its anti-apoptotic properties. this Viewpoint, we associate various functional studies on with structural reports, to decode unique behavior. well-structured N-terminus, compact barrel form, differences loop regions, specific transmembrane segments abundance thiols enable isoform perform different subset regulatory functions, establish features contribute gametogenesis. that demarcate it from suggest particular better suited regulating reactive oxygen species, steroidogenesis mitochondria-associated endoplasmic reticulum membrane pathways, ion forming secondary role. A understanding VDAC family will aid design inhibitors could alleviate irregularities VDAC-controlled pathways.

参考文章(25)
Heftsi Azoulay-Zohar, Claude Aflalo, Binding of rat brain hexokinase to recombinant yeast mitochondria: identification of necessary molecular determinants. Journal of Bioenergetics and Biomembranes. ,vol. 31, pp. 569- 579 ,(1999) , 10.1023/A:1005469028274
Jia Yuan, Ying Zhang, Yue Sheng, Xiazhou Fu, Hanhua Cheng, Rongjia Zhou, MYBL2 guides autophagy suppressor VDAC2 in the developing ovary to inhibit autophagy through a complex of VDAC2-BECN1-BCL2L1 in mammals. Autophagy. ,vol. 11, pp. 1081- 1098 ,(2015) , 10.1080/15548627.2015.1040970
Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi, N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry. Journal of Biological Chemistry. ,vol. 290, pp. 30240- 30252 ,(2015) , 10.1074/JBC.M115.693978
Masateru Okazaki, Katsue Kurabayashi, Miwako Asanuma, Yohei Saito, Kosuke Dodo, Mikiko Sodeoka, VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore Biochimica et Biophysica Acta. ,vol. 1848, pp. 3188- 3196 ,(2015) , 10.1016/J.BBAMEM.2015.09.017
Varda Shoshan-Barmatz, Danya Ben-Hail, Lee Admoni, Yakov Krelin, Shambhoo Sharan Tripathi, The mitochondrial voltage-dependent anion channel 1 in tumor cells. Biochimica et Biophysica Acta. ,vol. 1848, pp. 2547- 2575 ,(2015) , 10.1016/J.BBAMEM.2014.10.040
Johann Schredelseker, Aviv Paz, Carlos J. López, Christian Altenbach, Calvin S. Leung, Maria K. Drexler, Jau-Nian Chen, Wayne L. Hubbell, Jeff Abramson, High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population Journal of Biological Chemistry. ,vol. 289, pp. 12566- 12577 ,(2014) , 10.1074/JBC.M113.497438
Emily H-Y Cheng, Tatiana V Sheiko, Jill K Fisher, William J Craigen, Stanley J Korsmeyer, VDAC2 inhibits BAK activation and mitochondrial apoptosis. Science. ,vol. 301, pp. 513- 517 ,(2003) , 10.1126/SCIENCE.1083995
S. Abu-Hamad, N. Arbel, D. Calo, L. Arzoine, A. Israelson, N. Keinan, R. Ben-Romano, O. Friedman, V. Shoshan-Barmatz, The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins. Journal of Cell Science. ,vol. 122, pp. 1906- 1916 ,(2009) , 10.1242/JCS.040188
Nir Arbel, Danya Ben-Hail, Varda Shoshan-Barmatz, Mediation of the Antiapoptotic Activity of Bcl-xL Protein upon Interaction with VDAC1 Protein Journal of Biological Chemistry. ,vol. 287, pp. 23152- 23161 ,(2012) , 10.1074/JBC.M112.345918
Manoj Prasad, Jasmeet Kaur, Kevin J. Pawlak, Mahuya Bose, Randy M. Whittal, Himangshu S. Bose, Mitochondria-associated Endoplasmic Reticulum Membrane (MAM) Regulates Steroidogenic Activity via Steroidogenic Acute Regulatory Protein (StAR)-Voltage-dependent Anion Channel 2 (VDAC2) Interaction Journal of Biological Chemistry. ,vol. 290, pp. 2604- 2616 ,(2015) , 10.1074/JBC.M114.605808