Evidence map›Paper›PMID 11158326›Full record

ArticleMolecular and cellular biology2001

SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading.

N Prasad, R S Topping, S J Decker

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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.5field-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

42 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. PIPFEBS letters · 2022
    Article
  3. PTEN and Other PtdIns(3,4,5)PInternational journal of molecular sciences · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. PI3Kβ links integrin activation and PI(3,4)PMolecular biology of the cell · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Elevated expression of SHIP2 correlates with poor prognosis in non-small cell lung cancer.International journal of clinical and experimental pathology · 2013
    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

3 authors at 1 institution in 1 country.

N PrasadDepartment of Cell Biology, Pfizer Global Research and Development, Ann Arbor, Michigan 48105, USA.
R S Topping
S J Decker
Pfizer (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a previous study, we found that the SHIP2 protein became tyrosine phosphorylated and associated with the Shc adapter protein in response to the treatment of cells with growth factors and insulin (T. Habib, J. A. Hejna, R. E. Moses, and S. J. Decker, J. Biol. Chem. 273:18605-18609, 1998). We describe here a novel interaction between SHIP2 and the p130(Cas) adapter protein, a mediator of actin cytoskeleton organization. SHIP2 and p130(Cas) association was detected in anti-SHIP2 immunoprecipitates from several cell types. Reattachment of trypsinized cells stimulated tyrosine phosphorylation of SHIP2 and increased the formation of a complex containing SHIP2 and a faster-migrating tyrosine-phosphorylated form of p130(Cas). The faster-migrating form of p130(Cas) was no longer recognized by antibodies to the amino terminus of p130(Cas) and appeared to be generated through proteolysis. Interaction of the SHIP2 protein with the various forms of p130(Cas) was mediated primarily through the SH2 domain of SHIP2. Immunofluorescence studies indicated that SHIP2 localized to focal contacts and to lamellipodia. Increased adhesion was observed in HeLa cells transiently expressing exogenous WT-SHIP2. These effects were not seen with SHIP2 possessing a mutation in the SH2 domain (R47G). Transfection of a catalytic domain deletion mutant of SHIP2 (DeltaRV) inhibited cell spreading. Taken together, our studies suggest an important role for SHIP2 in adhesion and spreading.

Indexed as

ProteinsCell AdhesionCell LineCell MovementCrk-Associated Substrate ProteinHeLa CellsHumansMolecular WeightMutationPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoproteinsPhosphoric Monoester HydrolasesPhosphorylationRecombinant Fusion ProteinsRetinoblastoma-Like Protein p130src Homology DomainsBCAR1 protein, humanCrk-Associated Substrate ProteinINPPL1 protein, humanPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoproteinsPhosphoric Monoester HydrolasesProteinsRecombinant Fusion ProteinsRetinoblastoma-Like Protein p130Tyrosine

Identifiers

PMID11158326
PMCPMC99593
OpenAlexW2127074059

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.