Evidence map›Paper›PMID 22956996›Full record

ArticlePloS one2012

The minimal deneddylase core of the COP9 signalosome excludes the Csn6 MPN- domain.

Elah Pick, Amnon Golan, Jacob Z Zimbler, Liquan Guo, Yehonatan Sharaby, Tomohiko Tsuge, Kay Hofmann, Ning Wei

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In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Fungal COP9 signalosome assembly requires connection of two trimeric intermediates for integration of intrinsic deneddylase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  2. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  3. Biomolecules · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Elah PickDepartment of Biology, University of Haifa at Oranim, Tivon, Israel. elahpic@research.haifa.ac.il
Amnon Golan
Jacob Z Zimbler
Liquan Guo
Yehonatan Sharaby
Tomohiko Tsuge
Kay Hofmann
Ning Wei

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The COP9 signalosome (CSN) is a eukaryotic protein complex, which regulates a wide range of biological processes mainly through modulating the cullin ubiquitin E3 ligases in the ubiquitin-proteasome pathway. The CSN possesses a highly conserved deneddylase activity that centers at the JAMM motif of the Csn5 subunit but requires other subunits in a complex assembly. The classic CSN is composed of 8 subunits (Csn1-8), yet in several Ascomycota, the complex is smaller and lacks orthologs for a few CSN subunits, but nevertheless contains a conserved Csn5. This feature makes yeast a powerful model to determine the minimal assemblage required for deneddylation activity. Here we report, that Csi1, a diverged S. cerevisiae CSN subunit, displays significant homology with the carboxyl terminal domain of the canonical Csn6, but lacks the amino terminal MPN(-) domain. Through the comparative and experimental analyses of the budding yeast and the mammalian CSNs, we demonstrate that the MPN(-) domain of the canonical mouse Csn6 is not part of the CSN deneddylase core. We also show that the carboxyl domain of Csn6 has an indispensable role in maintaining the integrity of the CSN complex. The CSN complex assembled with the carboxyl fragment of Csn6, despite its lack of an MPN(-) domain, is fully active in deneddylation of cullins. We propose that the budding yeast Csi1 is a functional equivalent of the canonical Csn6, and thus the composition of the CSN across phyla is more conserved than hitherto appreciated.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsConserved SequenceCOP9 Signalosome ComplexCullin ProteinsHEK293 CellsHeLa CellsHumansMiceMolecular Sequence DataMultiprotein ComplexesMutagenesisPeptide HydrolasesProtein BindingProtein Structure, TertiaryCOP9 Signalosome ComplexCsi1 protein, S cerevisiaeCullin ProteinsMultiprotein ComplexesPeptide HydrolasesSaccharomyces cerevisiae Proteins

Identifiers

PMID22956996
PMCPMC3431379

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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.