Evidence map›Paper›PMID 11238916›Full record

ArticleMolecular and cellular biology2001

Protein tyrosine phosphatase phi regulates paxillin tyrosine phosphorylation and mediates colony-stimulating factor 1-induced morphological changes in macrophages.

F J Pixley, P S Lee, J S Condeelis, E R Stanley

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. The M-CSF receptor in osteoclasts and beyond.Experimental & molecular medicine · 2020
    Review
  7. Article
  8. Antigen SamplingFrontiers in immunology · 2019
    Article
  9. Review
  10. Article
  11. CSF-1R signaling in health and disease: a focus on the mammary gland.Journal of mammary gland biology and neoplasia · 2014
    Review
  12. CSF-1 receptor signaling in myeloid cells.Cold Spring Harbor perspectives in biology · 2014
    Review
  13. Review
  14. Article
  15. Article
  16. Macrophage Migration and Its Regulation by CSF-1.International journal of cell biology · 2012
    Article
  17. Article
  18. Review
  19. S100A4 regulates macrophage chemotaxis.Molecular biology of the cell · 2010
    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

4 authors at 2 institutions in 1 country.

F J PixleyDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
P S Lee
J S Condeelis
E R Stanley
Albert Einstein College of Medicine · USYeshiva University · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
REGULATION OF GRANULOCYTE AND MACROPHAGE PRODUCTIONR37CA026504 · NCI · YESHIVA UNIVERSITY · PI STANLEY, E. RICHARD · 1989 to 2011
$6.8M
HEMOPOIETIC STEM CELL DIFFERENTIATION TO MACROPHAGESR01CA032551 · NCI · YESHIVA UNIVERSITY · PI STANLEY, E. RICHARD · 1985 to 2013
$5.4M
SIGNAL TRANSDUCTION AND ACTIN DURING AMOEBOID CHEMOTAXISR01GM038511 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 1988 to 2008
$2.8M
REGULATION OF GRANULOCYTE AND MACROPHAGE PRODUCTIONR01CA026504 · NCI · YESHIVA UNIVERSITY · PI STANLEY, E RICHARD · 1985 to 2001
$1.2M
SPATIAL CONTROL OF PATHWAYS MEDIATING ACTIN DYNAMICSR01GM061034 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 2000 to 2003
$988k
NCI NIH HHS CA26504NCI NIH HHS CA32551NCI NIH HHS P30 CA013330NCI NIH HHS P-30-CA13330NCI NIH HHS R01 CA026504NCI NIH HHS R01 CA032551NCI NIH HHS R37 CA026504NIGMS NIH HHS GM38511NIGMS NIH HHS R01 GM038511NIGMS NIH HHS R01 GM061034
6 · The paper itself

Abstract

Removal of colony-stimulating factor 1 (CSF-1) causes macrophages to round up and to increase their expression of protein tyrosine phosphatase phi (PTP phi). This is accompanied by the disruption of focal complexes and the formation of ruffles. Here we have overexpressed wild-type (WT) PTP phi and a phosphatase-inactive (C325S) mutant in a macrophage cell line in the presence and absence of CSF-1. In the presence of CSF-1, WT PTP phi induces cell rounding and ruffle formation, while C325S PTP phi has no effect. In contrast, in CSF-1-starved cells, C325S PTP phi behaves in a dominant negative fashion, preventing rounding and ruffling. Furthermore, C325S PTP phi increases adhesion in cycling cells, while WT PTP phi enhances motility. In WT PTP phi-overexpressing cells, the focal contact protein paxillin is selectively depleted from focal complexes and specifically dephosphorylated on tyrosine. In contrast, paxillin is hyperphosphorylated in C325S PTP phi-expressing cells. Moreover, a complex containing PTP phi, paxillin, and a paxillin-associated tyrosine kinase, Pyk2, can be immunoprecipitated from macrophage lysates, and the catalytic domain of PTP phi selectively binds paxillin and Pyk2 in vitro. Although PTP phi and Pyk2 do not colocalize with paxillin in focal complexes, all three proteins are colocalized in dorsal ruffles. The results suggest that paxillin is dephosphorylated by PTP phi in dorsal ruffles, using Pyk2 as a bridging molecule, resulting in a reduced pool of tyrosine-phosphorylated paxillin available for incorporation into focal complexes, thereby mediating CSF-1 regulation of macrophage morphology, adhesion, and motility.

Indexed as

Blotting, WesternBrainCatalytic DomainCell AdhesionCell DivisionCell LineCell MovementCell SurvivalCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansKidneyMacrophage Colony-Stimulating FactorMacrophagesMicroscopy, FluorescenceCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMacrophage Colony-Stimulating FactorPaxillinPhosphoproteinsProtein IsoformsProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesPTK2 protein, humanPXN protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 3Tyrosine

Identifiers

PMID11238916
PMCPMC86738
OpenAlexW2089991028

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.