Evidence map›Paper›PMID 19875440›Full record

ArticleThe Journal of biological chemistry2010

Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.

Susan S Safadi, Gary S Shaw

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

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  11. Solution structure of the E3 ligase HOIL-1 Ubl domain.Protein science : a publication of the Protein Society · 2012
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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

2 authors at 1 institution in 1 country.

Susan S SafadiDepartment of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada.
Gary S Shaw
Western University · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only approximately 5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible alpha-helices each encompassing a UIM sequence. The alpha-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from beta1 and beta2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.

Indexed as

UbiquitinationAdaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SubstitutionCalcium-Binding ProteinsHumansIntracellular Signaling Peptides and ProteinsMagnetic Resonance SpectroscopyMutation, MissenseParkinsonian DisordersPhosphoproteinsProteasome Endopeptidase ComplexRNA-Binding ProteinsSignal TransductionUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingCalcium-Binding ProteinsEPS15 protein, humanIntracellular Signaling Peptides and Proteinsparkin proteinPhosphoproteinsProteasome Endopeptidase ComplexPSMD4 protein, humanRNA-Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID19875440
PMCPMC2801268
OpenAlexW2167911314

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.