Skip to main content
SpringerLink
Log in

Ubiquitin-proteasome system

Ubiquitin-free routes into the proteasome

  • Multi-author Review
  • Published:
Cellular and Molecular Life Sciences CMLS Aims and scope Submit manuscript

Abstract

The majority of proteasome substrates identified to date are marked for degradation by polyubiquitinylation. Exceptions to this principle, however, are well documented and can help us understand the process proteasomes use to recognize their substrates. Examples include ornithine decarboxylase, p21/Cip1, TCRα, IκBα, c-Jun, calmodulin and thymidylate synthase. Degradation of these proteins can be completely ubiquitin-independent or coexist with ubiquitin-dependent pathways. Uncoupling degradation from ubiquitin modification may reflect the evolutionary conservation of mechanisms optimized for highly specialized regulatory functions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Author information

Authors and Affiliations

  1. Department of Microbiology and Immunology, University of California, San Francisco, 94143-0414, San Francisco, California, USA

    M. A. Hoyt & P. Coffino

Authors
  1. M. A. Hoyt
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. P. Coffino
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to P. Coffino.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hoyt, M.A., Coffino, P. Ubiquitin-proteasome system. CMLS, Cell. Mol. Life Sci. 61, 1596–1600 (2004). https://doi.org/10.1007/s00018-004-4133-9

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00018-004-4133-9

Search

Navigation