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Ubiquitin chain elongation requires E3-dependent tracking of the emerging conjugate.
Kelly, Aileen; Wickliffe, Katherine E; Song, Ling; Fedrigo, Indro; Rape, Michael.
Afiliación
  • Kelly A; Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
  • Wickliffe KE; Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
  • Song L; Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
  • Fedrigo I; Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
  • Rape M; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA. Electronic address: mrape@berkeley.edu.
Mol Cell ; 56(2): 232-245, 2014 Oct 23.
Article en En | MEDLINE | ID: mdl-25306918
Protein modification with ubiquitin chains is an essential signaling event catalyzed by E3 ubiquitin ligases. Most human E3s contain a signature RING domain that recruits a ubiquitin-charged E2 and a separate domain for substrate recognition. How RING-E3s can build polymeric ubiquitin chains while binding substrates and E2s at defined interfaces remains poorly understood. Here, we show that the RING-E3 APC/C catalyzes chain elongation by strongly increasing the affinity of its E2 for the distal acceptor ubiquitin in a growing conjugate. This function of the APC/C requires its coactivator as well as conserved residues of the E2 and ubiquitin. APC/C's ability to track the tip of an emerging conjugate is required for APC/C-substrate degradation and accurate cell division. Our results suggest that RING-E3s tether the distal ubiquitin of a growing chain in proximity to the active site of their E2s, allowing them to assemble polymeric conjugates without altering their binding to substrate or E2.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitina / Enzimas Ubiquitina-Conjugadoras / Biosíntesis de Péptidos Independientes de Ácidos Nucleicos / Subunidad Apc11 del Ciclosoma-Complejo Promotor de la Anafase / Subunidad Apc2 del Ciclosoma-Complejo Promotor de la Anafase / Proteínas Cdc20 Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitina / Enzimas Ubiquitina-Conjugadoras / Biosíntesis de Péptidos Independientes de Ácidos Nucleicos / Subunidad Apc11 del Ciclosoma-Complejo Promotor de la Anafase / Subunidad Apc2 del Ciclosoma-Complejo Promotor de la Anafase / Proteínas Cdc20 Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos