VDAC-2 : Mitochondrial outer membrane regulator masquerading as a channel?
© 2015 Federation of European Biochemical Societies..
The voltage-dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such are required for cellular metabolism. The elaborate interplay between mitochondria and the apoptotic pathway supports a role for VDACs as a major regulator of cell death. Although VDAC-1 has an established role in apoptosis and cell homeostasis, the role of VDAC-2 has been controversial. In humans, VDAC-2 is best known for its anti-apoptotic properties. In this Viewpoint, we associate the various functional studies on VDAC-2 with structural reports, to decode its unique behavior. The well-structured N-terminus, compact barrel form, differences in the loop regions, specific transmembrane segments and the abundance of thiols in VDAC-2 enable this isoform to perform a different subset of regulatory functions, establish anti-apoptotic features and contribute to gametogenesis. VDAC-2 structural features that demarcate it from VDAC-1 suggest that this particular isoform is better suited for regulating reactive oxygen species, steroidogenesis and mitochondria-associated endoplasmic reticulum membrane regulatory pathways, with ion transport forming a secondary role. A better understanding of the unique structural features of the VDAC family will aid in the design of inhibitors that could alleviate irregularities in VDAC-controlled pathways.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2016 |
|---|---|
| Erschienen: |
2016 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:283 |
|---|---|
| Enthalten in: |
The FEBS journal - 283(2016), 10 vom: 11. Mai, Seite 1831-6 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Maurya, Svetlana Rajkumar [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 31.05.2017 Date Revised 29.01.2022 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1111/febs.13637 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM255949413 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM255949413 | ||
| 003 | DE-627 | ||
| 005 | 20231224175559.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231224s2016 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1111/febs.13637 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0853.xml |
| 035 | |a (DE-627)NLM255949413 | ||
| 035 | |a (NLM)26709731 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Maurya, Svetlana Rajkumar |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a VDAC-2 |b Mitochondrial outer membrane regulator masquerading as a channel? |
| 264 | 1 | |c 2016 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 31.05.2017 | ||
| 500 | |a Date Revised 29.01.2022 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2015 Federation of European Biochemical Societies. | ||
| 520 | |a The voltage-dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such are required for cellular metabolism. The elaborate interplay between mitochondria and the apoptotic pathway supports a role for VDACs as a major regulator of cell death. Although VDAC-1 has an established role in apoptosis and cell homeostasis, the role of VDAC-2 has been controversial. In humans, VDAC-2 is best known for its anti-apoptotic properties. In this Viewpoint, we associate the various functional studies on VDAC-2 with structural reports, to decode its unique behavior. The well-structured N-terminus, compact barrel form, differences in the loop regions, specific transmembrane segments and the abundance of thiols in VDAC-2 enable this isoform to perform a different subset of regulatory functions, establish anti-apoptotic features and contribute to gametogenesis. VDAC-2 structural features that demarcate it from VDAC-1 suggest that this particular isoform is better suited for regulating reactive oxygen species, steroidogenesis and mitochondria-associated endoplasmic reticulum membrane regulatory pathways, with ion transport forming a secondary role. A better understanding of the unique structural features of the VDAC family will aid in the design of inhibitors that could alleviate irregularities in VDAC-controlled pathways | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Review | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a apoptosis | |
| 650 | 4 | |a cysteines | |
| 650 | 4 | |a mitochondrial outer membrane | |
| 650 | 4 | |a voltage-dependent anion channel | |
| 650 | 4 | |a β-barrel proteins | |
| 650 | 7 | |a Ion Channels |2 NLM | |
| 650 | 7 | |a VDAC2 protein, human |2 NLM | |
| 650 | 7 | |a Voltage-Dependent Anion Channel 2 |2 NLM | |
| 700 | 1 | |a Mahalakshmi, Radhakrishnan |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The FEBS journal |d 2005 |g 283(2016), 10 vom: 11. Mai, Seite 1831-6 |w (DE-627)NLM15295631X |x 1742-4658 |7 nnns |
| 773 | 1 | 8 | |g volume:283 |g year:2016 |g number:10 |g day:11 |g month:05 |g pages:1831-6 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1111/febs.13637 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 283 |j 2016 |e 10 |b 11 |c 05 |h 1831-6 | ||