Historical Background
E3 ubiquitin ligases are a large family of proteins that recognize target substrates and mediate the transfer of ubiquitin from the E2 ubiquitin-conjugating enzyme to the substrate. These modifications can have diverse effects on the substrate, ranging from proteasome-dependent degradation to modulation of protein function, including activation and/or localization. The activity of most E3 ubiquitin ligases is specified by a RING domain, which is a protein structural domain of the zinc finger type containing a C3HC4amino acid motif. The mitochondrial ubiquitin ligase MITOL/MARCH5 belongs to the membrane-associated MARCH family of E3 ubiquitin ligases, which were originally discovered as structural homologs to Kaposi’s sarcoma-associated herpesvirus K3 and K5 ubiquitin E3 ligases. Hereafter, the term “MITOL” is used consistently when referring to this protein. MITOL is an...
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Tokuyama, T., Yanagi, S. (2016). Mitochondrial Ubiquitin Ligase MITOL/MARCH5. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101579-1
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DOI: https://doi.org/10.1007/978-1-4614-6438-9_101579-1
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