The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes
Open accessAbstract
Summary In mammals, fusion of the mitochondrial outer membrane is controlled by two DRPs, MFN1 and MFN2, that function in place of a single outer membrane DRP, Fzo1 in yeast. We addressed the significance of two mammalian outer membrane fusion DRPs using an in vitro mammalian mitochondrial fusion assay. We demonstrate that heterotypic MFN1/MFN2 trans complexes possess greater efficacy in fusion as compared to homotypic MFN1 or MFN2 complexes. In addition, we show that the soluble form of the pro-apoptotic Bcl2 protein, Bax, positively regulates mitochondrial fusion exclusively through homotypic MFN2 trans complexes. Together, these data demonstrate functional and regulatory distinctions between MFN1 and MFN2 and provide insight into their unique physiological roles.
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Cites
Genome-wide atlas of gene expression in the adult mouse brain
Lein, E. S., Hawrylycz, M. J., Ao, N., Ayres, M., Bensinger, A., Bernard, A., Boe, A. F., Boguski, M. S., Brockway, K. S., Byrnes, E. J., et al. (2007) · Nature · doi:10.1038/nature05453 · Cited by 5,572
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 4×
“…ª2011 Elsevier Inc. 157 expected, in the absence of GFP-Bax92-94Ala or GFP-Bax6365Ala expression, mitochondria were significantly fragmented in Mfn1+/+Mfn2 / and Mfn1 / Mfn2+/+ MEF cells as a consequence of an attenuation of fusion, as compared to wild-type cells (Figure 6B) (Chen et al., 2005).”
BackgroundResultInfluentialThe Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
Self-citationMitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731 · cited 1×
“Data from in vitro analyses suggest that MFN1 mediates mitochondrial tethering more efficiently than MFN2, suggesting the possibility that homotypic cis and trans MFN1 interactions may be more efficient and/or stable than the cognate MFN2 interactions (Ishihara et al., 2004).”
BackgroundRole of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625
Self-citationMitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0252 · Cited by 623 · cited 4×
“The Roles of Fusion DRPs We examined the roles of the outer and inner membrane fusion DRPs by analyzing mitochondria isolated from MEF-fusion DRP gene-knockout lines (Chen et al., 2003; Song et al., 2009).”
BackgroundResultInfluentialInducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515
Eura, Y. (2003) · Journal of Biochemistry · doi:10.1093/jb/mvg150 · Cited by 445 · cited 3×
“For example, MFN2 is the prevalent species in heart, skeletal muscle, and brain (Eura et al., 2003; Lein et al., 2007).”
Background
Cited by
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Self-citationMitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803
Self-citationMitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Del Re, D. P., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 961
Metadata
- Authors
- Hoppins, S., Edlich, F., Cleland, M. M., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 41
- Issue
- 2
- Pages
- 150-160
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1989554731
- Cited by
- 243
- References
- 11
- FWCI
- 9.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Hoppins, S., Edlich, F., Cleland, M. M., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. (2011). The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes. Molecular Cell. https://doi.org/10.1016/j.molcel.2010.11.030
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