Evidence map›Paper›PMID 22679023›Full record

Trial reportThe Journal of biological chemistry2012

The actin regulatory protein HS1 interacts with Arp2/3 and mediates efficient neutrophil chemotaxis.

Peter J Cavnar, Kevin Mogen, Erwin Berthier, David J Beebe, Anna Huttenlocher

Open access · hybridAbstract readClinical Trial
In one paragraph

Trial report in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Terpenoid balance inScience advances · 2024
    Article
  4. Article
  5. Terpenoid balance inbioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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 2 institutions in 1 country.

Peter J CavnarDepartments of Pediatrics and Medical Microbiology and Immunology, 4205 Microbial Sciences Building, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Kevin Mogen
Erwin Berthier
David J Beebe
Anna Huttenlocher
University of Wisconsin–Madison · USWisconsin Institutes for Discovery · US

Funding

UW COMPREHENSIVE CANCER CENTER SUPPORTP30CA014520 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI AMY TRENTHAM-DIETZ · 1985 to 2026
$142.6M
Molecular & Environmental Toxicology Pre-& Postdoctoral Training ProgramT32ES007015 · NIEHS · UNIVERSITY OF WISCONSIN-MADISON · PI CHRISTOPHER A BRADFIELD · 1985 to 2026
$11.5M
Understanding cell migration through microscale in vitro modelsR01EB010039 · NIBIB · UNIVERSITY OF WISCONSIN-MADISON · PI BEEBE, DAVID J, HUTTENLOCHER, ANNA · 2011 to 2014
$1.7M
NCI NIH HHS P30 CA014520NIBIB NIH HHS R01 EB010039NIBIB NIH HHS R01EB010039NIEHS NIH HHS T32 ES007015
6 · The paper itself

Abstract

HS1 is an actin regulatory protein and cortactin homolog that is expressed in hematopoietic cells. Antigen receptor stimulation induces HS1 phosphorylation, and HS1 is essential for T cell activation. HS1 is also expressed in neutrophils; however, the function of HS1 in neutrophils is not known. Here we show that HS1 localizes to the neutrophil leading edge, and is phosphorylated in response to the chemoattractant formyl-Met-Leu-Phe (fMLP) in adherent cells. Using live imaging in microchannels, we show that depletion of endogenous HS1 in the neutrophil-like PLB-985 cell line impairs chemotaxis. We also find that HS1 is necessary for chemoattractant-induced activation of Rac GTPase signaling and Vav1 phosphorylation, suggesting that HS1-mediated Rac activation is necessary for efficient neutrophil chemotaxis. We identify specific phosphorylation sites that mediate HS1-dependent neutrophil motility. Expression of HS1 Y378F, Y397F is sufficient to rescue migration of HS1-deficient neutrophils, however, a triple phospho-mutant Y222F, Y378F, Y397F did not rescue migration of HS1-deficient neutrophils. Moreover, HS1 phosphorylation on Y222, Y378, and Y397 regulates its interaction with Arp2/3. Collectively, our findings identify a novel role for HS1 and its phosphorylation during neutrophil directed migration.

Indexed as

Actin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingAmino Acid SubstitutionBlood ProteinsCell LineChemotaxisFemaleHumansMaleMutation, MissenseNeutrophilsN-Formylmethionine Leucyl-PhenylalaninePhosphorylationProto-Oncogene Proteins c-vavrac GTP-Binding ProteinsSignal TransductionActin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingBlood ProteinsHCLS1 protein, humanN-Formylmethionine Leucyl-PhenylalanineProto-Oncogene Proteins c-vavrac GTP-Binding ProteinsVAV1 protein, human

Identifiers

PMID22679023
PMCPMC3408136
OpenAlexW2164204231

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.