Evidence map›Paper›PMID 10613908›Full record

ArticleThe Journal of cell biology1999

An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles.

A E Engqvist-Goldstein, M M Kessels, V S Chopra, M R Hayden, D G Drubin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 216 citations in OpenAlex.

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  8. Huntingtin-interacting protein family members have a conserved pro-viral function fromProceedings of the National Academy of Sciences of the United States of America · 2020
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18 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

5 authors at 2 institutions in 2 countries.

A E Engqvist-GoldsteinDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California 94720-3202, USA.
M M Kessels
V S Chopra
M R Hayden
D G Drubin
University of California, Berkeley · USUniversity of British Columbia · CA

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
NIDDK NIH HHS DK32094NIDDK NIH HHS P01 DK032094NIGMS NIH HHS GM50399NIGMS NIH HHS R01 GM050399
6 · The paper itself

Abstract

The actin cytoskeleton has been implicated in endocytosis, yet few molecules that link these systems have been identified. Here, we have cloned and characterized mHip1R, a protein that is closely related to huntingtin interacting protein 1 (Hip1). These two proteins are mammalian homologues of Sla2p, an actin binding protein important for actin organization and endocytosis in yeast. Sequence alignments and secondary structure predictions verified that mHip1R belongs to the Sla2 protein family. Thus, mHip1R contains an NH(2)-terminal domain homologous to that implicated in Sla2p's endocytic function, three predicted coiled-coils, a leucine zipper, and a talin-like actin-binding domain at the COOH terminus. The talin-like domain of mHip1R binds to F-actin in vitro and colocalizes with F-actin in vivo, indicating that this activity has been conserved from yeast to mammals. mHip1R shows a punctate immunolocalization and is enriched at the cell cortex and in the perinuclear region. We concluded that the cortical localization represents endocytic compartments, because mHip1R colocalizes with clathrin, AP-2, and endocytosed transferrin, and because mHip1R fractionates biochemically with clathrin-coated vesicles. Time-lapse video microscopy of mHip1R-green fluorescence protein (GFP) revealed a blinking behavior similar to that reported for GFP-clathrin, and an actin-dependent inward movement of punctate structures from the cell periphery. These data show that mHip1R is a component of clathrin-coated pits and vesicles and suggest that it might link the endocytic machinery to the actin cytoskeleton.

Indexed as

DNA-Binding ProteinsSaccharomyces cerevisiae Proteins3T3 CellsActinsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCarrier ProteinsCoated Pits, Cell-MembraneCoated VesiclesCOS CellsCytoskeletal ProteinsCytoskeletonDetergentsDogsEndocytosisActinsAdaptor Proteins, Signal TransducingCarrier ProteinsCytoskeletal ProteinsDetergentsDNA-Binding ProteinsFungal ProteinsHIP1 protein, humanHip1 protein, mouseHip1r protein, mouseMembrane ProteinsMicrofilament ProteinsSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiaeTalin

Identifiers

PMID10613908
PMCPMC2174256
OpenAlexW1997312506

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.