Evidence map›Paper›PMID 8089175›Full record

ArticleThe Journal of cell biology1994

Ponticulin is an atypical membrane protein.

A L Hitt, T H Lu, E J Luna

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 53 citations in OpenAlex.

  1. RNABMC genomics · 2021
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  13. Ordered yeast artificial chromosome clones representing the Dictyostelium discoideum genome.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
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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.

A L HittWorcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
T H Lu
E J Luna

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
CELL BIOLOGY OF DEVELOPMENTT32HD007312 · NICHD · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI RICHTER, JOEL D · 1985 to 2010
$1.9M
ACTIN-BINDING MEMBRANE PROTEINS IN INVASIVE CELLSR55CA054885 · NCI · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1991 to 1991
–
NCI NIH HHS CA54885NICHD NIH HHS T32HD07312NIGMS NIH HHS GM33048NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

We have cloned and sequenced ponticulin, a 17,000-dalton integral membrane glycoprotein that binds F-actin and nucleates actin assembly. A single copy gene encodes a developmentally regulated message that is high during growth and early development, but drops precipitously during cell streaming at approximately 8 h of development. The deduced amino acid sequence predicts a protein with a cleaved NH2-terminal signal sequence and a COOH-terminal glycosyl anchor. These predictions are supported by amino acid sequencing of mature ponticulin and metabolic labeling with glycosyl anchor components. Although no alpha-helical membrane-spanning domains are apparent, several hydrophobic and/or sided beta-strands, each long enough to traverse the membrane, are predicted. Although its location on the primary sequence is unclear, an intracellular domain is indicated by the existence of a discontinuous epitope that is accessible to antibody in plasma membranes and permeabilized cells, but not in intact cells. Such a cytoplasmically oriented domain also is required for the demonstrated role of ponticulin in binding actin to the plasma membrane in vivo and in vitro (Hitt, A. L., J. H. Hartwig, and E. J. Luna. 1994. Ponticulin is the major high affinity link between the plasma membrane and the cortical actin network in Dictyostelium. J. Cell Biol. 126:1433-1444). Thus, ponticulin apparently represents a new category of integral membrane proteins that consists of proteins with both a glycosyl anchor and membrane-spanning peptide domain(s).

Indexed as

Amino Acid SequenceAnimalsBase SequenceCarrier ProteinsCytoplasmDictyosteliumFungal ProteinsGenomic LibraryGlycosylphosphatidylinositolsMembrane GlycoproteinsMicrofilament ProteinsMolecular Sequence DataPolymerase Chain ReactionProtein Structure, SecondaryCarrier ProteinsF-actin-binding proteinsFungal ProteinsGlycosylphosphatidylinositolsMembrane GlycoproteinsMicrofilament Proteins

Identifiers

PMID8089175
PMCPMC2290967
OpenAlexW2013279274

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.