The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
Open accessAbstract
Protein secretion from the endoplasmic reticulum (ER) requires the enzymatic activity of chaperones and oxidoreductases that fold polypeptides and form disulfide bonds within newly synthesized proteins. The best-characterized ER redox relay depends on the transfer of oxidizing equivalents from molecular oxygen through ER oxidoreductin 1 (Ero1) and protein disulfide isomerase to nascent polypeptides. The formation of disulfide bonds is, however, not the sole function of ER oxidoreductases, which are also important regulators of ER calcium homeostasis. Given the role of human Ero1alpha in the regulation of the calcium release by inositol 1,4,5-trisphosphate receptors during the onset of apoptosis, we hypothesized that Ero1alpha may have a redox-sensitive localization to specific domains of the ER. Our results show that within the ER, Ero1alpha is almost exclusively found on the mitochondria-associated membrane (MAM). The localization of Ero1alpha on the MAM is dependent on oxidizing conditions within the ER. Chemical reduction of the ER environment, but not ER stress in general leads to release of Ero1alpha from the MAM. In addition, the correct localization of Ero1alpha to the MAM also requires normoxic conditions, but not ongoing oxidative phosphorylation.
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Cites
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., & Helenius, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00494-5 · Cited by 221
May, D., Itin, A., Gal, O., Kalinski, H., Feinstein, E., & Keshet, E. (2005) · Oncogene · doi:10.1038/sj.onc.1208325 · Cited by 167
Cited by
PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress
Verfaillie, T., Rubio, N., Garg, A. D., Bultynck, G., Rizzuto, R., Decuypere, J.-P., Piette, J., Linehan, C., Gupta, S., Samali, A., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.74 · Cited by 850
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 625
Self-citationOrganization and Function of Membrane Contact Sites
Helle, S. C. J., Kanfer, G., Kolar, K., Lang, A., Michel, A. H., & Kornmann, B. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.028 · Cited by 453
Metadata
- Authors
- Gilady, S. Y., Bui, M., Lynes, E. M., Benson, M. D., Watts, R., Vance, J. E., & Simmen, T.
- Venue
- Cell Stress and Chaperones
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 15
- Issue
- 5
- Pages
- 619-629
- ISSN
- 1355-8145 (ISSN-L)
- OpenAlex
- W2084938264
- Cited by
- 173
- References
- 3
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gilady, S. Y., Bui, M., Lynes, E. M., Benson, M. D., Watts, R., Vance, J. E., & Simmen, T. (2010). Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress and Chaperones. https://doi.org/10.1007/s12192-010-0174-1
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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