Evidence map›Paper›PMID 17522383›Full record

ArticleMolecular biology of the cell2007

Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.

Sarah L Barker, Linda Lee, B Daniel Pierce, Lymarie Maldonado-Báez, David G Drubin, Beverly Wendland

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

26 citing papers in PubMed, 42 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

6 authors at 2 institutions in 1 country.

Sarah L BarkerDepartment of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA.
Linda Lee
B Daniel Pierce
Lymarie Maldonado-Báez
David G Drubin
Beverly Wendland
Johns Hopkins University · USUniversity of California, Berkeley · US

Funding

MOLECULAR ANALYSIS OF ENDOCYTOSIS PROTEINS IN YEASTR01GM060979 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WENDLAND, BEVERLY R · 2000 to 2013
$4.3M
Molecular Analysis of the Yeast Actin CytoskeletonR37GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 2006 to 2015
$4.0M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
NIGMS NIH HHS GM-42759NIGMS NIH HHS GM-60979NIGMS NIH HHS R01 GM042759NIGMS NIH HHS R01 GM060979NIGMS NIH HHS R37 GM042759
6 · The paper itself

Abstract

The yeast endocytic scaffold Pan1 contains an uncharacterized proline-rich domain (PRD) at its carboxy (C)-terminus. We report that the pan1-20 temperature-sensitive allele has a disrupted PRD due to a frame-shift mutation in the open reading frame of the domain. To reveal redundantly masked functions of the PRD, synthetic genetic array screens with a pan1DeltaPRD strain found genetic interactions with alleles of ACT1, LAS17 and a deletion of SLA1. Through a yeast two-hybrid screen, the Src homology 3 domains of the type I myosins, Myo3 and Myo5, were identified as binding partners for the C-terminus of Pan1. In vitro and in vivo assays validated this interaction. The relative timing of recruitment of Pan1-green fluorescent protein (GFP) and Myo3/5-red fluorescent protein (RFP) at nascent endocytic sites was revealed by two-color real-time fluorescence microscopy; the type I myosins join Pan1 at cortical patches at a late stage of internalization, preceding the inward movement of Pan1 and its disassembly. In cells lacking the Pan1 PRD, we observed an increased lifetime of Myo5-GFP at the cortex. Finally, Pan1 PRD enhanced the actin polymerization activity of Myo5-Vrp1 complexes in vitro. We propose that Pan1 and the type I myosins interactions promote an actin activity important at a late stage in endocytic internalization.

Indexed as

EndocytosisActin-Related Protein 2-3 ComplexActinsAllelesAmino Acid SequenceAnimalsFungal ProteinsMicrofilament ProteinsMolecular Sequence DataMyosin Type IProtein BindingProtein Structure, TertiaryProtein TransportRabbitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActin-Related Protein 2-3 ComplexActinsFungal ProteinsMicrofilament ProteinsMyosin Type IPAN1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID17522383
PMCPMC1949359
OpenAlexW2123918295

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.