Evidence map›Paper›PMID 19828733›Full record

ArticleMolecular biology of the cell2009

Requirements for recruitment of a G protein-coupled receptor to clathrin-coated pits in budding yeast.

Junko Y Toshima, Jun-ichi Nakanishi, Kensaku Mizuno, Jiro Toshima, David G Drubin

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

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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

5 authors at 3 institutions in 2 countries.

Junko Y ToshimaDepartment of Biological Science and Technology, Tokyo University of Science, Yamazaki 2641, Noda, Chiba 278-8510, Japan.
Jun-ichi Nakanishi
Kensaku Mizuno
Jiro Toshima
David G Drubin
Tokyo University of Science · JPTohoku University · JPUniversity of California, Berkeley · US

Funding

The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
NIGMS NIH HHS GM-R0150399
6 · The paper itself

Abstract

Endocytic internalization of G protein-coupled receptors (GPCRs) plays a critical role in down-regulation of GPCR signaling. The yeast mating pheromone receptor Ste2p has been used as a model to investigate mechanisms of signal transduction, modification, and endocytic internalization of GPCRs. We previously used a fluorescently labeled mating pheromone derivative to reveal unappreciated molecular and spatiotemporal features of GPCR endocytosis in budding yeast. Here, we identify recruitment of Ste2p to preexisting clathrin-coated pits (CCPs) as a key step regulated by receptor phosphorylation and subsequent ubiquitination upon ligand binding. The yeast casein kinase I homologue Yck2p directly phosphorylates six serine residues located in the C-terminal tail of Ste2p, and mutation of these serine residues to alanine significantly decreased recruitment of Ste2p to CCPs. We also found that the clathrin adaptors Ent1p, Ent2p, and Ede1p work cooperatively to recruit ubiquitinated Ste2p to CCPs. In addition, ubiquitination has a role in ligand-independent constitutive recruitment of Ste2p to CCPs, although this process is much slower than ligand-induced recruitment. These results suggest that ubiquitination of Ste2p is indispensable for recruiting Ste2p to CCPs in both ligand-dependent and ligand-independent endocytosis.

Indexed as

Amino Acid MotifsAmino Acid SequenceClathrinCoated Pits, Cell-MembraneEndocytosisLigandsMolecular Sequence DataPhosphorylationProtein BindingProtein PrecursorsProtein Structure, TertiaryProtein TransportReceptors, G-Protein-CoupledSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime FactorsClathrinLigandsMF(ALPHA)1 protein, S cerevisiaeProtein PrecursorsReceptors, G-Protein-CoupledSaccharomyces cerevisiae ProteinsUbiquitinated Proteins

Identifiers

PMID19828733
PMCPMC2793282
OpenAlexW1989285948

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.