Evidence map›Paper›PMID 1522116›Full record

ArticleThe Journal of cell biology1992

The lymphocyte-specific protein LSP1 binds to F-actin and to the cytoskeleton through its COOH-terminal basic domain.

J Jongstra-Bilen, P A Janmey, J H Hartwig, S Galea, J Jongstra

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.

  1. Blood pressure loci identified with a gene-centric array.American journal of human genetics · 2011
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Leukocyte-specific protein 1 regulates neutrophil recruitment in acute lung inflammation.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Hairy cell leukemia.Medical oncology (Northwood, London, England) · 2007
    Review
  19. Review
  20. Article
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 1 institution in 1 country.

J Jongstra-BilenDepartment of Immunology, University of Toronto, Ontario, Canada.
P A Janmey
J H Hartwig
S Galea
J Jongstra
University of Toronto · CA

Funding

REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR01AR038910 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 1991 to 2006
$2.2M
REGULATION OF PLATELET SHAPE CHANGESR01HL047874 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI HARTWIG, JOHN H · 1991 to 1993
–
REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR29AR038910 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI JANMEY, PAUL A · 1987 to 1989
–
NHLBI NIH HHS HL47874NIAMS NIH HHS AR38910
6 · The paper itself

Abstract

The lymphocyte-specific phosphoprotein LSP1 associates with the cytoplasmic face of the plasma membrane and with the cytoskeleton. Mouse LSP1 protein contains 330 amino acids and contains an NH2-terminal acidic domain of approximately 177 amino acids. The COOH-terminal half of the LSP1 protein is rich in basic residues. In this paper we show that LSP1 protein which is immunoprecipitated with anti-LSP1 antibodies from NP-40-soluble lysates of the mouse B-lymphoma cell line BAL17 is associated with actin. In vitro binding experiments using recombinant LSP1 (rLSP1) protein and rabbit skeletal muscle actin show that LSP1 binds along the sides of F-actin but does not bind to G-actin. rLSP1 does not alter the initial polymerization kinetics of actin. The highly conserved COOH-terminal basic domains of mouse and human LSP1 share a significant homology with the 20-kD COOH-terminal F-actin binding fragment of caldesmon. A truncated rLSP1 protein containing the entire COOH-terminal basic domain from residue 179 to 330, but not the NH2-terminal acidic domain binds to F-actin at least as well as rLSP1. When LSP1/CAT fusion proteins are expressed in a LSP1-negative T-lymphoma cell line, only fusion proteins containing the basic COOH-terminal domain associate with the NP-40-insoluble cytoskeleton. These data show that LSP1 binds F-actin through its COOH-terminal basic domain and strongly suggest that LSP1 interacts with the cytoskeleton by direct binding to F-actin. We propose that LSP1 plays a role in mediating cytoskeleton driven responses in lymphocytes such as receptor capping, cell motility, or cell-cell interactions.

Indexed as

ActinsAmino Acid SequenceAnimalsBlotting, WesternCalcium-Binding ProteinsCytoskeletonFluorescent Antibody TechniqueKineticsMiceMicrofilament ProteinsMicroscopy, ElectronMolecular Sequence DataPhosphoproteinsRabbitsRecombinant ProteinsTumor Cells, CulturedActinsCalcium-Binding ProteinsLSP1 protein, humanLsp1 protein, mouseMicrofilament ProteinsPhosphoproteinsRecombinant Proteins

Identifiers

PMID1522116
PMCPMC2289610
OpenAlexW2121613672

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.