For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
47
views
422
references
 Top references
cited by
159
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      483
      similar
       All similar
      • Record: found
      • Abstract: not found
      • Article: not found

      The Ubiquitin–Proteasome System ofSaccharomyces cerevisiae

      Author(s): , , ,
      Publication date Created:
      Publication date (Electronic):
      Journal: Genetics
      Publisher: Genetics Society of America

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.

          Related collections

          Most cited references422

          • Record: found
          • Abstract: found
          • Article: not found

          Systematic and quantitative assessment of the ubiquitin-modified proteome.

          Woong Kim, Eric J. Bennett, Edward L. Huttlin … (2011)
          Despite the diverse biological pathways known to be regulated by ubiquitylation, global identification of substrates that are targeted for ubiquitylation has remained a challenge. To globally characterize the human ubiquitin-modified proteome (ubiquitinome), we utilized a monoclonal antibody that recognizes diglycine (diGly)-containing isopeptides following trypsin digestion. We identify ~19,000 diGly-modified lysine residues within ~5000 proteins. Using quantitative proteomics we monitored temporal changes in diGly site abundance in response to both proteasomal and translational inhibition, indicating both a dependence on ongoing translation to observe alterations in site abundance and distinct dynamics of individual modified lysines in response to proteasome inhibition. Further, we demonstrate that quantitative diGly proteomics can be utilized to identify substrates for cullin-RING ubiquitin ligases. Interrogation of the ubiquitinome allows for not only a quantitative assessment of alterations in protein homeostasis fidelity, but also identification of substrates for individual ubiquitin pathway enzymes. Copyright © 2011 Elsevier Inc. All rights reserved.
          Article 0 comments Cited 611 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Dynamics and diversity in autophagy mechanisms: lessons from yeast.

            Hitoshi Nakatogawa, Kuninori Suzuki, Yoshiaki Kamada … (2009)
            Autophagy is a fundamental function of eukaryotic cells and is well conserved from yeast to humans. The most remarkable feature of autophagy is the synthesis of double membrane-bound compartments that sequester materials to be degraded in lytic compartments, a process that seems to be mechanistically distinct from conventional membrane traffic. The discovery of autophagy in yeast and the genetic tractability of this organism have allowed us to identify genes that are responsible for this process, which has led to the explosive growth of this research field seen today. Analyses of autophagy-related (Atg) proteins have unveiled dynamic and diverse aspects of mechanisms that underlie membrane formation during autophagy.
            Article 0 comments Cited 550 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.

              Carsten Hoege, Boris Pfander, George-Lucian Moldovan … (2002)
              The RAD6 pathway is central to post-replicative DNA repair in eukaryotic cells; however, the machinery and its regulation remain poorly understood. Two principal elements of this pathway are the ubiquitin-conjugating enzymes RAD6 and the MMS2-UBC13 heterodimer, which are recruited to chromatin by the RING-finger proteins RAD18 and RAD5, respectively. Here we show that UBC9, a small ubiquitin-related modifier (SUMO)-conjugating enzyme, is also affiliated with this pathway and that proliferating cell nuclear antigen (PCNA) -- a DNA-polymerase sliding clamp involved in DNA synthesis and repair -- is a substrate. PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination--which additionally requires MMS2, UBC13 and RAD5--and is conjugated to SUMO by UBC9. All three modifications affect the same lysine residue of PCNA, suggesting that they label PCNA for alternative functions. We demonstrate that these modifications differentially affect resistance to DNA damage, and that damage-induced PCNA ubiquitination is elementary for DNA repair and occurs at the same conserved residue in yeast and humans.
              Article 0 comments Cited 537 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Title: Genetics
                Abbreviated Title: Genetics
                Publisher: Genetics Society of America
                ISSN (Print): 0016-6731
                ISSN (Electronic): 1943-2631
                Publication date Created: October 01 2012
                Publication date Created: October 2012
                Publication date (Electronic): October 01 2012
                Publication date (Print): October 2012
                Volume: 192
                Issue: 2
                Pages: 319-360
                Article
                DOI: 10.1534/genetics.112.140467
                PMC ID: 3454868
                PubMed ID: 23028185
                SO-VID: 7479f2f0-965e-4012-b117-814b37df70bf
                Copyright © © 2012
                History

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content483

                See all similar

                Cited by158

                See all cited by

                Most referenced authors4,905

                See all reference authors