Evidence map›Paper›PMID 19387488›Full record

ArticleThe EMBO journal2009

S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains.

Hyoung Tae Kim, Kwang Pyo Kim, Tomoaki Uchiki, Steven P Gygi, Alfred L Goldberg

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
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  8. The recognition of ubiquitinated proteins by the proteasome.Cellular and molecular life sciences : CMLS · 2016
    Review
  9. Article
  10. Ubiquitin modifications.Cell research · 2016
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 2 countries.

Hyoung Tae KimDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Kwang Pyo Kim
Tomoaki Uchiki
Steven P Gygi
Alfred L Goldberg
Harvard University · US

Funding

MOLECULAR CHAPERONES AND PROTEIN DEGRADATIONR01GM051923 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1995 to 2020
$10.1M
NIGMS NIH HHS R01 GM051923
6 · The paper itself

Abstract

Ubiquitin (Ub)-protein conjugates formed by purified ring-finger or U-box E3s with the E2, UbcH5, resist degradation and disassembly by 26S proteasomes. These chains contain multiple types of Ub forks in which two Ub's are linked to adjacent lysines on the proximal Ub. We tested whether cells contain factors that prevent formation of nondegradable conjugates and whether the forked chains prevent proteasomal degradation. S5a is a ubiquitin interacting motif (UIM) protein present in the cytosol and in the 26S proteasome. Addition of S5a or a GST-fusion of S5a's UIM domains to a ubiquitination reaction containing 26S proteasomes, UbcH5, an E3 (MuRF1 or CHIP), and a protein substrate, dramatically stimulated its degradation, provided S5a was present during ubiquitination. Mass spectrometry showed that S5a and GST-UIM prevented the formation of Ub forks without affecting synthesis of standard isopeptide linkages. The forked Ub chains bind poorly to 26S proteasomes unlike those synthesized with S5a present or linked to Lys63 or Lys48 chains. Thus, S5a (and presumably certain other UIM proteins) function with certain E3/E2 pairs to ensure synthesis of efficiently degraded non-forked Ub conjugates.

Indexed as

HumansLuciferasesLysineMutationProteasome Endopeptidase ComplexProtein Structure, TertiaryRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTroponin IUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesLuciferasesLysineProteasome Endopeptidase ComplexPSMD4 protein, humanRNA-Binding ProteinsRPN10 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTroponin IUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

PMID19387488
PMCPMC2711177
OpenAlexW2126539283

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.