Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-07

AUTHORS

Domagoj Vucic, Vishva M. Dixit, Ingrid E. Wertz

ABSTRACT

The proper regulation of apoptosis is essential for the survival of multicellular organisms. Furthermore, excessive apoptosis can contribute to neurodegenerative diseases, anaemia and graft rejection, and diminished apoptosis can lead to autoimmune diseases and cancer. It has become clear that the post-translational modification of apoptotic proteins by ubiquitylation regulates key components in cell death signalling cascades. For example, ubiquitin E3 ligases, such as MDM2 (which ubiquitylates p53) and inhibitor of apoptosis (IAP) proteins, and deubiquitinases, such as A20 and ubiquitin-specific protease 9X (USP9X) (which regulate the ubiquitylation and degradation of receptor-interacting protein 1 (RIP1) and myeloid leukaemia cell differentiation 1 (MCL1), respectively), have important roles in apoptosis. Therapeutic agents that target apoptotic regulatory proteins, including those that are part of the ubiquitin-proteasome system, might afford clinical benefits. More... »

PAGES

439

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nrm3143

    DOI

    http://dx.doi.org/10.1038/nrm3143

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1049207587

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/21697901


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