Evidence map›Paper›PMID 16873553›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The WD40 and FYVE domain containing protein 2 defines a class of early endosomes necessary for endocytosis.

Akira Hayakawa, Deborah Leonard, Stephanie Murphy, Susan Hayes, Martha Soto, Kevin Fogarty, Clive Standley, Karl Bellve, David Lambright, Craig Mello and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

32 citing papers in PubMed, 54 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

11 authors at 2 institutions in 2 countries.

Akira HayakawaProgram in Molecular Medicine and Biomedical Imaging Group, Department of Physiology, University of Massachusetts Medical School, Worcester, MA 01615, USA.
Deborah Leonard
Stephanie Murphy
Susan Hayes
Martha Soto
Kevin Fogarty
Clive Standley
Karl Bellve
David Lambright
Craig Mello
Silvia Corvera
Institute of Molecular Medicine · INUniversity of Massachusetts Chan Medical School · US

Funding

PILOT AND FEASIBILITY PROGRAMP30DK032520 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CZECH, MICHAEL P · 1986 to 2010
$14.6M
SUBCELLULAR LOCALIZATION OF PI 3-KINASE SIGNALINGP01DK060564 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FOGARTY, KEVIN EDWARD · 2001 to 2011
$13.9M
PI3 KINASE EFFECTORS IN INSULIN RESPONSIVE SYSTEMSR01DK054479 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CORVERA, SILVIA · 1998 to 2010
$2.9M
NIDDK NIH HHS DK32520NIDDK NIH HHS DK60564NIDDK NIH HHS P01 DK060564NIDDK NIH HHS P30 DK032520NIDDK NIH HHS R01 DK054479PHS HHS DDK54479
6 · The paper itself

Abstract

The FYVE domain binds with high specificity and avidity to phosphatidylinositol 3-phosphate. It is present in approximately 30 proteins in humans, some of which have been implicated in functions ranging from early endosome fusion to signal transduction through the TGF-beta receptor. To develop a further understanding of the biological roles of this protein family, we turned to the nematode Caenorhabditis elegans, which contains only 12 genes predicted to encode for phosphatidylinositol 3-phosphate binding, FYVE domain-containing proteins, all of which have homologs in the human genome. Each of these proteins was targeted individually by RNA interference. One protein, WDFY2, produced a strong inhibition of endocytosis when silenced. WDFY2 contains WD40 motifs and a FYVE domain, is highly conserved between species, and localizes to a set of small endosomes that reside within 100 nm from the plasma membrane. These endosomes are involved in transferrin uptake but lack the classical endosomal markers Rab5 and EEA1. Silencing of WDFY2 by siRNA in mammalian cells impaired transferrin endocytosis. These studies reveal the important, conserved role of WDFY2 in endocytosis, and the existence of a subset of early endosomes, closely associated with the plasma membrane, that may constitute the first stage of endocytic processing of internalized cargo.

Indexed as

EndocytosisAmino Acid SequenceAnimalsCaenorhabditis elegansCell MembraneChlorocebus aethiopsCOS CellsEndosomesGreen Fluorescent ProteinsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataPhosphatidylinositol PhosphatesProtein Structure, TertiaryGreen Fluorescent ProteinsIntracellular Signaling Peptides and Proteinsphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesWDFY2 protein, human

Identifiers

PMID16873553
PMCPMC1567675
OpenAlexW2051868705

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.