[{"department":[{"_id":"LeSa"}],"date_updated":"2023-08-02T06:55:42Z","status":"public","type":"journal_article","article_type":"original","_id":"10182","volume":23,"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["1471-0072"],"eissn":["1471-0080"]},"intvolume":" 23","month":"02","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"text":"The mitochondrial oxidative phosphorylation system is central to cellular metabolism. It comprises five enzymatic complexes and two mobile electron carriers that work in a mitochondrial respiratory chain. By coupling the oxidation of reducing equivalents coming into mitochondria to the generation and subsequent dissipation of a proton gradient across the inner mitochondrial membrane, this electron transport chain drives the production of ATP, which is then used as a primary energy carrier in virtually all cellular processes. Minimal perturbations of the respiratory chain activity are linked to diseases; therefore, it is necessary to understand how these complexes are assembled and regulated and how they function. In this Review, we outline the latest assembly models for each individual complex, and we also highlight the recent discoveries indicating that the formation of larger assemblies, known as respiratory supercomplexes, originates from the association of the intermediates of individual complexes. We then discuss how recent cryo-electron microscopy structures have been key to answering open questions on the function of the electron transport chain in mitochondrial respiration and how supercomplexes and other factors, including metabolites, can regulate the activity of the single complexes. When relevant, we discuss how these mechanisms contribute to physiology and outline their deregulation in human diseases.","lang":"eng"}],"title":"The assembly, regulation and function of the mitochondrial respiratory chain","external_id":{"pmid":["34621061"],"isi":["000705697100001"]},"article_processing_charge":"No","author":[{"orcid":" 0000-0001-5618-3449","full_name":"Vercellino, Irene","last_name":"Vercellino","first_name":"Irene","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989","last_name":"Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","first_name":"Leonid A"}],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","citation":{"mla":"Vercellino, Irene, and Leonid A. Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular Cell Biology, vol. 23, Springer Nature, 2022, pp. 141–161, doi:10.1038/s41580-021-00415-0.","ama":"Vercellino I, Sazanov LA. The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 2022;23:141–161. doi:10.1038/s41580-021-00415-0","apa":"Vercellino, I., & Sazanov, L. A. (2022). The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/s41580-021-00415-0","short":"I. Vercellino, L.A. Sazanov, Nature Reviews Molecular Cell Biology 23 (2022) 141–161.","ieee":"I. Vercellino and L. A. Sazanov, “The assembly, regulation and function of the mitochondrial respiratory chain,” Nature Reviews Molecular Cell Biology, vol. 23. Springer Nature, pp. 141–161, 2022.","chicago":"Vercellino, Irene, and Leonid A Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular Cell Biology. Springer Nature, 2022. https://doi.org/10.1038/s41580-021-00415-0.","ista":"Vercellino I, Sazanov LA. 2022. The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 23, 141–161."},"date_created":"2021-10-24T22:01:35Z","date_published":"2022-02-01T00:00:00Z","doi":"10.1038/s41580-021-00415-0","page":"141–161","publication":"Nature Reviews Molecular Cell Biology","day":"01","year":"2022","isi":1,"quality_controlled":"1","publisher":"Springer Nature"},{"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","citation":{"mla":"Yamada, KM, and Michael K. Sixt. “Mechanisms of 3D Cell Migration.” Nature Reviews Molecular Cell Biology, vol. 20, no. 12, Springer Nature, 2019, pp. 738–752, doi:10.1038/s41580-019-0172-9.","ama":"Yamada K, Sixt MK. Mechanisms of 3D cell migration. Nature Reviews Molecular Cell Biology. 2019;20(12):738–752. doi:10.1038/s41580-019-0172-9","apa":"Yamada, K., & Sixt, M. K. (2019). Mechanisms of 3D cell migration. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/s41580-019-0172-9","short":"K. Yamada, M.K. Sixt, Nature Reviews Molecular Cell Biology 20 (2019) 738–752.","ieee":"K. Yamada and M. K. Sixt, “Mechanisms of 3D cell migration,” Nature Reviews Molecular Cell Biology, vol. 20, no. 12. Springer Nature, pp. 738–752, 2019.","chicago":"Yamada, KM, and Michael K Sixt. “Mechanisms of 3D Cell Migration.” Nature Reviews Molecular Cell Biology. Springer Nature, 2019. https://doi.org/10.1038/s41580-019-0172-9.","ista":"Yamada K, Sixt MK. 2019. Mechanisms of 3D cell migration. Nature Reviews Molecular Cell Biology. 20(12), 738–752."},"title":"Mechanisms of 3D cell migration","author":[{"last_name":"Yamada","full_name":"Yamada, KM","first_name":"KM"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K"}],"article_processing_charge":"No","external_id":{"pmid":["31582855"],"isi":["000497966900007"]},"day":"01","publication":"Nature Reviews Molecular Cell Biology","isi":1,"year":"2019","doi":"10.1038/s41580-019-0172-9","date_published":"2019-12-01T00:00:00Z","date_created":"2019-11-12T14:54:42Z","page":"738–752","quality_controlled":"1","publisher":"Springer Nature","date_updated":"2023-08-30T07:22:20Z","department":[{"_id":"MiSi"}],"_id":"7009","status":"public","type":"journal_article","article_type":"review","language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1471-0080"],"issn":["1471-0072"]},"publication_status":"published","issue":"12","volume":20,"oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"Cell migration is essential for physiological processes as diverse as development, immune defence and wound healing. It is also a hallmark of cancer malignancy. Thousands of publications have elucidated detailed molecular and biophysical mechanisms of cultured cells migrating on flat, 2D substrates of glass and plastic. However, much less is known about how cells successfully navigate the complex 3D environments of living tissues. In these more complex, native environments, cells use multiple modes of migration, including mesenchymal, amoeboid, lobopodial and collective, and these are governed by the local extracellular microenvironment, specific modalities of Rho GTPase signalling and non- muscle myosin contractility. Migration through 3D environments is challenging because it requires the cell to squeeze through complex or dense extracellular structures. Doing so requires specific cellular adaptations to mechanical features of the extracellular matrix (ECM) or its remodelling. In addition, besides navigating through diverse ECM environments and overcoming extracellular barriers, cells often interact with neighbouring cells and tissues through physical and signalling interactions. Accordingly, cells need to call on an impressively wide diversity of mechanisms to meet these challenges. This Review examines how cells use both classical and novel mechanisms of locomotion as they traverse challenging 3D matrices and cellular environments. It focuses on principles rather than details of migratory mechanisms and draws comparisons between 1D, 2D and 3D migration."}],"month":"12","intvolume":" 20","scopus_import":"1"},{"page":"55-61","date_published":"2013-01-01T00:00:00Z","doi":"10.1038/nrm3496","date_created":"2022-04-07T07:50:43Z","year":"2013","day":"01","publication":"Nature Reviews Molecular Cell Biology","quality_controlled":"1","publisher":"Springer Nature","author":[{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_processing_charge":"No","external_id":{"pmid":["23258296"]},"title":"Protein homeostasis: Live long, won't prosper","citation":{"chicago":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” Nature Reviews Molecular Cell Biology. Springer Nature, 2013. https://doi.org/10.1038/nrm3496.","ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61.","mla":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” Nature Reviews Molecular Cell Biology, vol. 14, Springer Nature, 2013, pp. 55–61, doi:10.1038/nrm3496.","apa":"Toyama, B. H., & Hetzer, M. (2013). Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/nrm3496","ama":"Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 2013;14:55-61. doi:10.1038/nrm3496","ieee":"B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,” Nature Reviews Molecular Cell Biology, vol. 14. Springer Nature, pp. 55–61, 2013.","short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","volume":14,"publication_identifier":{"issn":["1471-0072","1471-0080"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","month":"01","intvolume":" 14","abstract":[{"lang":"eng","text":"Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular proteins, however, have been identified that evade this turnover process and instead are maintained over a cell's lifetime. This diverse group of long-lived proteins might be particularly prone to accumulation of damage and thus have a crucial role in the functional deterioration of key regulatory processes during ageing."}],"oa_version":"None","pmid":1,"date_updated":"2022-07-18T08:37:53Z","extern":"1","article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology","Molecular Biology"],"_id":"11084"}]