Evidence map›Paper›PMID 11352928›Full record

ArticleThe Journal of cell biology2001

Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease.

S B Helliwell, S Losko, C A Kaiser

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 267 citations in OpenAlex.

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57 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

S B HelliwellDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
S Losko
C A Kaiser
Massachusetts Institute of Technology · US

Funding

REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANER01GM056933 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KAISER, CHRIS ALAN · 1998 to 2010
$3.1M
NIGMS NIH HHS GM56933NIGMS NIH HHS R01 GM056933
6 · The paper itself

Abstract

Gap1p, the general amino acid permease of Saccharomyces cerevisiae, is regulated by intracellular sorting decisions that occur in either Golgi or endosomal compartments. Depending on nitrogen source, Gap1p is transported to the plasma membrane, where it functions for amino acid uptake, or to the vacuole, where it is degraded. We found that overexpression of Bul1p or Bul2p, two nonessential components of the Rsp5p E3-ubiquitin ligase complex, causes Gap1p to be sorted to the vacuole regardless of nitrogen source. The double mutant bul1Delta bul2Delta has the inverse phenotype, causing Gap1p to be delivered to the plasma membrane more efficiently than in wild-type cells. In addition, bul1Delta bul2Delta can reverse the effect of lst4Delta, a mutation that normally prevents Gap1p from reaching the plasma membrane. Evaluation of Gap1p ubiquitination revealed a prominent polyubiquitinated species that was greatly diminished in a bul1Delta bul2Delta mutant. Both a rsp5-1 mutant and a COOH-terminal truncation of Gap1p behave as bul1Delta bul2Delta, causing constitutive delivery of Gap1p to the plasma membrane and decreasing Gap1p polyubiquitination. These results indicate that Bul1p and Bul2p, together with Rsp5p, generate a polyubiquitin signal on Gap1p that specifies its intracellular targeting to the vacuole.

Indexed as

Adaptor Proteins, Signal TransducingSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesAmino Acid Transport SystemsCarbon RadioisotopesCarrier ProteinsCitrullineEndosomal Sorting Complexes Required for TransportGene DeletionGene Expression Regulation, EnzymologicGene Expression Regulation, FungalGolgi ApparatusLigasesMembrane Transport ProteinsPlasmidsProtein Structure, TertiaryAdaptor Proteins, Signal TransducingAmino Acid Transport SystemsBUL1 protein, S cerevisiaeBUL2 protein, S cerevisiaeCarbon RadioisotopesCarrier ProteinsCitrullineEndosomal Sorting Complexes Required for TransportLigasesMembrane Transport ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID11352928
PMCPMC2192387
OpenAlexW2136816588

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.