Evidence map›Paper›PMID 26161950›Full record

ArticleBiochemistry2015

Prb1 Protease Activity Is Required for Its Recognition by the F-Box Protein Saf1.

Kevin G Mark, Fernando Meza-Gutierrez, Jeffrey R Johnson, Billy W Newton, Nevan J Krogan, David P Toczyski

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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

1 citing paper in PubMed.

  1. Genetic interaction between RLM1 and F-box motif encoding gene SAF1 contributes to stress response in Saccharomyces cerevisiae.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2021
    Article
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.

Kevin G Mark†Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158, United States.
Fernando Meza-Gutierrez†Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158, United States.
Jeffrey R Johnson‡Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, United States.
Billy W Newton‡Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, United States.
Nevan J Krogan‡Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, United States.
David P Toczyski†Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158, United States.

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
Rewiring Therapeutic Cells: User-Controlled T Cells and Stem CellsP50GM081879 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2010 to 2017
$19.0M
Regulation by post-translation modifications in response to stressR35GM118104 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI TOCZYSKI, DAVID PAUL · 2016 to 2025
$7.2M
Comparative Analysis of Genetic Interaction NetworksR01GM084279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI IDEKER, TREY, KROGAN, NEVAN J · 2008 to 2017
$3.9M
Structure and function of the APCR01GM070539 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI TOCZYSKI, DAVID PAUL · 2004 to 2015
$3.9M
Physical and Genetic Interaction Landscape of the Tyrosine KinomeR01GM107671 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BANDYOPADHYAY, SOURAV · 2014 to 2017
$1.8M
NIAID NIH HHS P30 AI027763NIGMS NIH HHS GM070539NIGMS NIH HHS GM081879NIGMS NIH HHS GM084279NIGMS NIH HHS GM107671NIGMS NIH HHS P50 GM081879NIGMS NIH HHS R01 GM070539NIGMS NIH HHS R01 GM084279NIGMS NIH HHS R01 GM107671NIGMS NIH HHS R35 GM118104
6 · The paper itself

Abstract

The SCF ubiquitin ligase associates with substrates through its F-box protein adaptor. Substrates are typically recognized through a defined phosphodegron. Here, we characterize the interaction of the F-box protein Saf1 with Prb1, one of its vacuolar protease substrates. We show that Saf1 binds the mature protein but ubiquitinates only the zymogen precursor. The ubiquitinated lysine was found to be in a peptide eliminated from the mature protein. Mutations that eliminate the catalytic activity of Prb1, or the related substrate Prc1, block Saf1 targeting of the zymogen precursor. Our data suggest that Saf1 does not require a conventional degron as do other F-box proteins but instead recognizes the catalytic site itself.

Indexed as

EndopeptidasesF-Box ProteinsProtein BindingProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndopeptidasesF-Box ProteinsPRB1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSaf1 protein, S cerevisiae

Identifiers

PMID26161950
PMCPMC4816488

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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.