Evidence map›Paper›PMID 19942853›Full record

ArticleThe EMBO journal2009

Cullin neddylation and substrate-adaptors counteract SCF inhibition by the CAND1-like protein Lag2 in Saccharomyces cerevisiae.

Edyta Siergiejuk, Daniel C Scott, Brenda A Schulman, Kay Hofmann, Thimo Kurz, Matthias Peter

Abstract 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

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  8. The NEDD8 modification pathway in plants.Frontiers in plant science · 2014
    Review
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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

6 authors at 4 institutions in 4 countries.

Edyta SiergiejukETH Zürich, Institute of Biochemistry, Schafmattstrasse 18, Zürich, Switzerland.
Daniel C Scott
Brenda A Schulman
Kay Hofmann
Thimo Kurz
Matthias Peter
ETH Zurich · CHHoward Hughes Medical Institute · USMiltenyi Biotec (Germany) · DESt. Jude Children's Research Hospital · US

Funding

Ubiquitin-like Protein Transfer CascadesR01GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2013
$3.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM069530NIGMS NIH HHS R01GM069530
6 · The paper itself

Abstract

Cullin-based E3 ubiquitin ligases are activated through covalent modification of the cullin subunit by the ubiquitin-like protein Nedd8. Cullin neddylation dissociates the ligase assembly inhibitor Cand1, and promotes E2 recruitment and ubiquitin transfer by inducing a conformational change. Here, we have identified and characterized Lag2 as a likely Saccharomyces cerevisiae orthologue of mammalian Cand1. Similar to Cand1, Lag2 directly interacts with non-neddylated yeast cullin Cdc53 and prevents its neddylation in vivo and in vitro. Binding occurs through a conserved C-terminal beta-hairpin structure that inserts into the Skp1-binding pocket on the cullin, and an N-terminal motif that covers the neddylation lysine. Interestingly, Lag2 is itself neddylated in vivo on a lysine adjacent to this N-terminal-binding site. Overexpression of Lag2 inhibits Cdc53 activity in strains defective for Skp1 or neddylation functions, implying that these activities are important to counteract Lag2 in vivo. Our results favour a model in which binding of substrate-specific adaptors triggers release of Cand1/Lag2, whereas subsequent neddylation of the cullin facilitates the removal and prevents re-association of Lag2/Cand1.

Indexed as

Gene Expression Regulation, FungalAmino Acid SequenceBinding SitesCullin ProteinsModels, BiologicalMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesCdc53 protein, S cerevisiaeCullin ProteinsLAG2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID19942853
PMCPMC2797064
OpenAlexW2074676459

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.