Mitochondrial VDAC and Its Complexes

Brdiczka, Dieter

doi:10.1002/9783527621095.ch6

Cited by 4 publications

(7 citation statements)

References 144 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been proposed that tubulin is a component of a supercomplex referred to as the ATP synthasome, containing MtCK, VDAC and tubulin, and found at contact sites that regulate respiration and energy fluxes in heart (Brdiczka, 2007;Timohhina et al, 2009). VDAC1 was furthermore reported to interact with other cytoskeletal proteins.…”

Section: Vdac Interaction With and Regulation By Cytoskeletal Proteinsmentioning

confidence: 99%

VDAC, a multi-functional mitochondrial protein regulating cell life and death

Shoshan‐Barmatz

Pinto

Zweckstetter

et al. 2010

Molecular Aspects of Medicine

665

731

View full text Add to dashboard Cite

Section: Vdac Interaction With and Regulation By Cytoskeletal Proteinsmentioning

confidence: 99%

VDAC, a multi-functional mitochondrial protein regulating cell life and death

Shoshan‐Barmatz

Pinto

Zweckstetter

et al. 2010

Molecular Aspects of Medicine

665

731

View full text Add to dashboard Cite

“…(i) Contact sites, as estimated from electron micrographs of freeze-fractured mitochondria of rat livers, exist transiently and depend on energy state [57,243,365]. Their number is minima!…”

Section: H-b State 3 Respiration: Cardiolipbz-pnm'#t Interactions: mentioning

confidence: 99%

Cardiolipins and biomembrane function

Hoch

1992

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes

569

373

View full text Add to dashboard Cite

Evidence is discussed for roles of cardiolipins in oxidative phosphorylation mechanisms that regulate State 4 respiration by returning ejected protons across and over bacterial and mitochondrial membrane phospholipids, and that regulate State 3 respiration through the relative contributions of proteins that transport protons, electrons and/or metabolites. The barrier properties of phospholipid bilayers support and regulate the slow proton leak that is the basis for State 4 respiration. Proton permeability is in the range 10(-3)-10(-4) cm s-1 in mitochondria and in protein-free membranes formed from extracted mitochondrial phospholipids or from stable synthetic phosphatidylcholines or phosphatidylethanolamines. The roles of cardiolipins in proton conductance in model phospholipid membrane systems need to be assessed in view of new findings by Hübner et al. [313]: saturated cardiolipins form bilayers whilst natural highly unsaturated cardiolipins form nonlamellar phases. Mitochondrial cardiolipins apparently participate in bilayers formed by phosphatidylcholines and phosphatidylethanolamines. It is not yet clear if cardiolipins themselves conduct protons back across the membrane according to their degree of fatty acyl saturation, and/or modulate proton conductance by phosphatidylcholines and phosphatidylethanolamines. Mitochondrial cardiolipins, especially those with high 18:2 acyl contents, strongly bind many carrier and enzyme proteins that are involved in oxidative phosphorylation, some of which contribute to regulation of State 3 respiration. The role of cardiolipins in biomembrane protein function has been examined by measuring retained phospholipids and phospholipid binding in purified proteins, and by reconstituting delipidated proteins. The reconstitution criterion for the significance of cardiolipin-protein interactions has been catalytical activity; proton-pumping and multiprotein interactions have yet to be correlated. Some proteins, e.g., cytochrome c oxidase are catalytically active when dimyristoylphosphatidylcholine replaces retained cardiolipins. Cardiolipin-protein interactions orient membrane proteins, matrix proteins, and on the outerface receptors, enzymes, and some leader peptides for import; activate enzymes or keep them inactive unless the inner membrane is disrupted; and modulate formation of nonbilayer HII-phases. The capacity of the proton-exchanging uncoupling protein to accelerate thermogenic respiration in brown adipose tissue mitochondria of cold-adapted animals is not apparently affected by the increased cardiolipin unsaturation; this protein seems to take over the protonophoric role of cardiolipins in other mitochondria. Many in vivo influences that affect proton leakage and carrier rates selectively alter cardiolipins in amount per mitochondrial phospholipids, in fatty acyl composition and perhaps in sidedness; other mitochondrial membrane phospholipids respond less or not at all.(ABSTRACT TRUNCATED AT 400 WORDS)

show abstract

“…hexokinase, which affects the phosphorylation of glucose and thus the rate of glycolysis (Brdiczka, 2007). Thus, through the formation of complexes with ANT, CK and hexokinase, VDAC links oxidative phosphorylation with glycolysis.…”

Section: Regulation Of Energy Metabolism Through the Phosphocreatine mentioning

confidence: 99%

“…The mitochondrial isoform of CK also forms complexes with VDAC and the adenine nucleotide transporter (ANT) (Brdiczka, 2007). VDACs are generally involved in the transport of organic anions, mitochondrial metabolites, ( phospho-) creatine, ATP, ADP and inorganic phosphate (P i ) across the outer mitochondrial membrane, which raises the possibility that the closure of these channels regulates the overall activity of the mitochondrion (Lemasters and Holmuhamedov, 2006;Lemasters et al, 2012).…”

Section: Regulation Of Energy Metabolism Through the Phosphocreatine mentioning

confidence: 99%

“…However, VDAC2b increased in 26°C-acclimated fish and might therefore have a distinct role from VDAC2a. VDACs are also part of the mitochondrial permeability transition (MPT) pore, which might play a role during the mitochondrial pathway of apoptosis (Brdiczka, 2007). VDAC2, possibly as part of the MPT pore, can inhibit the activation of mitochondrial apoptosis (Cheng et al, 2003).…”

Section: Regulation Of Energy Metabolism Through the Phosphocreatine mentioning

confidence: 99%

See 1 more Smart Citation

Proteomic analysis of cardiac response to thermal acclimation in the eurythermal goby fishGillichthys mirabilis

Jayasundara

Tomanek

Dowd

et al. 2015

Journal of Experimental Biology

View full text Add to dashboard Cite

Cardiac function is thought to play a central role in determining thermal optima and tolerance limits in teleost fishes. Investigating proteomic responses to temperature in cardiac tissues may provide insights into mechanisms supporting the thermal plasticity of cardiac function. Here, we utilized a global proteomic analysis to investigate changes in cardiac protein abundance in response to temperature acclimation (transfer from 13°C to 9, 19 and 26°C) in a eurythermal goby, Gillichthys mirabilis. Proteomic data revealed 122 differentially expressed proteins across acclimation groups, 37 of which were identified using tandem mass-spectrometry. These 37 proteins are involved in energy metabolism, mitochondrial regulation, iron homeostasis, cytoprotection against hypoxia, and cytoskeletal organization. Compared with the 9 and 26°C groups, proteins involved in energy metabolism increased in 19°C-acclimated fish, indicating an overall increase in the capacity for ATP production. Creatine kinase abundance increased in 9°C-acclimated fish, suggesting an important role for the phosphocreatine energy shuttle in cold-acclimated hearts. Both 9 and 26°C fish also increased abundance of hexosaminidase, a protein directly involved in posthypoxia stress cytoprotection of cardiac tissues. Cytoskeletal restructuring appears to occur in all acclimation groups; however, the most prominent effect was detected in 26°C-acclimated fish, which exhibited significantly increased actin levels. Overall, proteomic analysis of cardiac tissue suggests that the capacity to adjust ATP-generating processes is crucial to the thermal plasticity of cardiac function. Furthermore, G. mirabilis may optimize cellular functions at temperatures near 19°C, which lies within the species' preferred temperature range.

show abstract

Mitochondrial VDAC and Its Complexes

Cited by 4 publications

References 144 publications

VDAC, a multi-functional mitochondrial protein regulating cell life and death

VDAC, a multi-functional mitochondrial protein regulating cell life and death

Cardiolipins and biomembrane function

Proteomic analysis of cardiac response to thermal acclimation in the eurythermal goby fishGillichthys mirabilis

Contact Info

Product

Resources

About