Evidence map›Paper›PMID 25694450›Full record

ArticleMolecular biology of the cell2015

Control of lipid organization and actin assembly during clathrin-mediated endocytosis by the cytoplasmic tail of the rhomboid protein Rbd2.

Christa L Cortesio, Eric B Lewellyn, David G Drubin

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 13 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

3 authors at 1 institution in 1 country.

Christa L CortesioDepartment of Molecular- and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.
Eric B LewellynDepartment of Molecular- and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.
David G DrubinDepartment of Molecular- and Cell Biology, University of California, Berkeley, Berkeley, CA 94720 drubin@berkeley.edu.
University of California, Berkeley · US

Funding

The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
Regulatory Mechanisms of yeast WASP Recruitment and Activity During EndocytosisF32GM097876 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CORTESIO, CHRISTA LINLEIGH · 2011 to 2013
$148k
Understanding the role of myosin in endocytosisF32GM100709 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI LEWELLYN, ERIC BRECHER · 2012 to 2013
$101k
NIGMS NIH HHS F32 GM097876NIGMS NIH HHS F32 GM100709NIGMS NIH HHS R01 GM042759NIGMS NIH HHS R01 GM050399NIGMS NIH HHS R01 GM42759NIGMS NIH HHS R01 GM50399
6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is facilitated by a precisely regulated burst of actin assembly. PtdIns(4,5)P2 is an important signaling lipid with conserved roles in CME and actin assembly regulation. Rhomboid family multipass transmembrane proteins regulate diverse cellular processes; however, rhomboid-mediated CME regulation has not been described. We report that yeast lacking the rhomboid protein Rbd2 exhibit accelerated endocytic-site dynamics and premature actin assembly during CME through a PtdIns(4,5)P2-dependent mechanism. Combined genetic and biochemical studies showed that the cytoplasmic tail of Rbd2 binds directly to PtdIns(4,5)P2 and is sufficient for Rbd2's role in actin regulation. Analysis of an Rbd2 mutant with diminished PtdIns(4,5)P2-binding capacity indicates that this interaction is necessary for the temporal regulation of actin assembly during CME. The cytoplasmic tail of Rbd2 appears to modulate PtdIns(4,5)P2 distribution on the cell cortex. The syndapin-like F-BAR protein Bzz1 functions in a pathway with Rbd2 to control the timing of type 1 myosin recruitment and actin polymerization onset during CME. This work reveals that the previously unstudied rhomboid protein Rbd2 functions in vivo at the nexus of three highly conserved processes: lipid regulation, endocytic regulation, and cytoskeletal function.

Indexed as

ClathrinActin CytoskeletonCell MembraneEndocytosisMicrofilament ProteinsMyosinsPeptide HydrolasesPhosphatidylinositol 4,5-DiphosphateSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionBzz1 protein, S cerevisiaeClathrinMicrofilament ProteinsMyosinsPeptide HydrolasesPhosphatidylinositol 4,5-DiphosphateRbd2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25694450
PMCPMC4395130
OpenAlexW2050426111

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.