Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane

Pinto, Vito De; Messina, Angela; Lane, Darius J.R.; Lawen, Alfons

doi:10.1016/j.febslet.2010.02.049

Cited by 154 publications

(136 citation statements)

References 77 publications

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“…3A, Hsp60, which is known to predominantly reside in the matrix, was also detected in the matrix with trace amounts detected in the OM and IM fractions (lanes 2 and 4), a finding consistent with those reported by others that Hsp60 can be detected at other sites (35)(36)(37). VDAC1 is known to reside in the mitochondrial OM and has been reported to also localize to other subcellular sites, including plasma membrane and the ER (38,39). As expected, VDAC1 was found in the OM fraction but not in the IMS or M fraction, although it was also detected in the IM fraction (Fig.…”

Section: Chcm1/chchd6 Is a Novel Mitochondrial Protein-wesupporting

confidence: 78%

CHCM1/CHCHD6, Novel Mitochondrial Protein Linked to Regulation of Mitofilin and Mitochondrial Cristae Morphology

Shi

et al. 2012

Journal of Biological Chemistry

114

134

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Background: Functional characterization of a novel mitochondrial protein, CHCM1/CHCHD6, is reported. Results: CHCM1 interacts with Mitofilin, DISC1, and CHCHD3, and its deficiency leads to severe defects in mitochondrial cristae morphology, reduction in cell growth, ATP production, and oxygen consumption. Conclusion: CHCM1/CHCHD6 is a novel player linked to mitochondrial cristae morphology. Significance: Results provide valuable insights into molecular events controlling the structural integrity and biogenesis of mitochondrial cristae.

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Section: Chcm1/chchd6 Is a Novel Mitochondrial Protein-wesupporting

confidence: 78%

CHCM1/CHCHD6, Novel Mitochondrial Protein Linked to Regulation of Mitofilin and Mitochondrial Cristae Morphology

Shi

et al. 2012

Journal of Biological Chemistry

114

134

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“…Hence, FISH can be coupled to immunofluorescence, and it is possible to quantitatively monitor mitochondrial DNA, RNA and proteins simultaneously. The mitochondrial porin VDAC is frequently used for assessing the mitochondrial mass (Acquaviva et al, 2005), but its presence elsewhere than in mitochondria (De Pinto et al, 2010, see also supplementary material Fig. S1) led us to use TOM22 instead (Fig.…”

Section: Mtrip Reveals Heterogeneity In Mitochondrial Transcriptionmentioning

confidence: 99%

Large heterogeneity of mitochondrial DNA transcription and initiation of replication exposed by single-cell imaging

Châtre

Ricchetti

2012

Journal of Cell Science

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SummaryMitochondrial DNA (mtDNA) replication and transcription are crucial for cell function, but these processes are poorly understood at the single-cell level. We describe a novel fluorescence in situ hybridization protocol, called mTRIP (mitochondrial transcription and replication imaging protocol), that reveals simultaneously mtDNA and RNA, and that can also be coupled to immunofluorescence for in situ protein examination. mTRIP reveals mitochondrial structures engaged in initiation of DNA replication by identification of a specific sequence in the regulatory D-loop, as well as unique transcription profiles in single human cells. We observe and quantify at least three classes of mitochondrial structures: (i) replication initiation active and transcript-positive (Ia-Tp); (ii) replication initiation silent and transcript-positive (Is-Tp); and (iii) replication initiation silent and transcript-negative (Is-Tn). Thus, individual mitochondria are dramatically heterogeneous within the same cell. Moreover, mTRIP exposes a mosaic of distinct nucleic acid patterns in the D-loop, including H-strand versus L-strand transcripts, and uncoupled rRNA transcription and mtDNA initiation of replication, which might have functional consequences in the regulation of the mtDNA. Finally, mTRIP identifies altered mtDNA processing in cells with unbalanced mtDNA content and function, including in human mitochondrial disorders. Thus, mTRIP reveals qualitative and quantitative alterations that provide additional tools for elucidating the dynamics of mtDNA processing in single cells and mitochondrial dysfunction in diseases.

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“…VDAC2 was originally characterized as a mitochondrial porin; however, 31 kDa VDAC2 proteins have also been enriched from the plasma membrane fraction of human B lymphocytes (Pinto et al 2010, Sabirov & Merzlyak 2012. Based on a recent proteomic study on human mesenchymal stromal cell surfaces, the presence of VDAC2 in the plasma membrane has also been suggested (Niehage et al 2011).…”

Section: Discussionmentioning

confidence: 99%

Sperm activation by heat shock protein 70 supports the migration of sperm released from sperm storage tubules in Japanese quail (Coturnix japonica)

Hiyama¹,

Matsuzaki²,

Mizushima³

et al. 2014

Reproduction

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Systems for maintaining the viability of ejaculated sperm in the female reproductive tract are widespread among vertebrates and invertebrates. In birds, this sperm storage function is performed by specialized simple tubular invaginations called sperm storage tubules (SSTs) in the uterovaginal junction (UVJ) of the oviduct. Although the incidence and physiological reasons for sperm storage in birds have been reported extensively, the mechanisms of sperm uptake by the SSTs, sperm maintenance within the SSTs, and control of sperm release from the SSTs are poorly understood. In this study, we demonstrated that the highly conserved heat shock protein 70 (HSP70) stimulates sperm motility in vitro and also that HSP70 expressed in the UVJ may facilitate the migration of sperm released from the SSTs.Quantitative RT-PCR analysis demonstrated that the expression of HSP70 mRNA in the UVJ increases before ovulation/oviposition. Gene-specific in situ hybridization and immunohistochemical analysis with a specific antibody to HSP70 demonstrated that HSP70 is localized in the surface epithelium of the UVJ. Furthermore, injection of anti-HSP70 antibody into the vagina significantly inhibited fertilization in vivo. In addition, we found that recombinant HSP70 activates flagellar movement in the sperm and that the binding of recombinant HSP70 to the sperm surface is mediated through an interaction with voltage-dependent anion channel protein 2 (VDAC2). Our results suggest that HSP70 binds to the sperm surface by interacting with VDAC2 and activating sperm motility. This binding appears to play an important role in sperm migration within the oviduct.

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Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane

Cited by 154 publications

References 77 publications

CHCM1/CHCHD6, Novel Mitochondrial Protein Linked to Regulation of Mitofilin and Mitochondrial Cristae Morphology

CHCM1/CHCHD6, Novel Mitochondrial Protein Linked to Regulation of Mitofilin and Mitochondrial Cristae Morphology

Large heterogeneity of mitochondrial DNA transcription and initiation of replication exposed by single-cell imaging

Sperm activation by heat shock protein 70 supports the migration of sperm released from sperm storage tubules in Japanese quail (Coturnix japonica)

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