Evidence map›Paper›PMID 9265651›Full record

ArticleThe Journal of cell biology1997

PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase.

S Spencer, D Dowbenko, J Cheng, W Li, J Brush, S Utzig, V Simanis, L A Lasky

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 167 citations in OpenAlex.

  1. Review
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  5. Article
  6. Review
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  8. Review
  9. Article
  10. Article
  11. The Contribution of PTPN22 to Rheumatic Disease.Arthritis & rheumatology (Hoboken, N.J.) · 2019
    Review
  12. Article
  13. Article
  14. Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Tyrosine phosphatase inhibition induces an ASC-dependent pyroptosis.Biochemical and biophysical research communications · 2012
    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

8 authors at 1 institution in 1 country.

S SpencerDepartment of Molecular Oncology, Genentech, Inc., South San Francisco, California 94080, USA.
D Dowbenko
J Cheng
W Li
J Brush
S Utzig
V Simanis
L A Lasky
Molecular Oncology (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated proteins which interact with the PEST-type protein tyrosine phosphatase, PTP hematopoietic stem cell fraction (HSCF), using the yeast two-hybrid system. This resulted in the identification of proline, serine, threonine phosphatase interacting protein (PSTPIP), a novel member of the actin- associated protein family that is homologous to Schizosaccharomyces pombe CDC15p, a phosphorylated protein involved with the assembly of the actin ring in the cytokinetic cleavage furrow. The binding of PTP HSCF to PSTPIP was induced by a novel interaction between the putative coiled-coil region of PSTPIP and the COOH-terminal, proline-rich region of the phosphatase. PSTPIP is tyrosine phosphorylated both endogenously and in v-Src transfected COS cells, and cotransfection of dominant-negative PTP HSCF results in hyperphosphorylation of PSTPIP. This dominant-negative effect is dependent upon the inclusion of the COOH-terminal, proline-rich PSTPIP-binding region of the phosphatase. Confocal microscopy analysis of endogenous PSTPIP revealed colocalization with the cortical actin cytoskeleton, lamellipodia, and actin-rich cytokinetic cleavage furrow. Overexpression of PSTPIP in 3T3 cells resulted in the formation of extended filopodia, consistent with a role for this protein in actin reorganization. Finally, overexpression of mammalian PSTPIP in exponentially growing S. pombe results in a dominant-negative inhibition of cytokinesis. PSTPIP is therefore a novel actin-associated protein, potentially involved with cytokinesis, whose tyrosine phosphorylation is regulated by PTP HSCF.

Indexed as

Adaptor Proteins, Signal Transducing3T3 CellsActinsAmino Acid SequenceAnimalsCarrier ProteinsCell CycleCytoskeletal ProteinsDrug InteractionsHematopoietic Cell Growth FactorsMiceMolecular Sequence DataPhosphorylationProtein BindingProtein Tyrosine Phosphatase, Non-Receptor Type 12Protein Tyrosine PhosphatasesActinsAdaptor Proteins, Signal TransducingCarrier ProteinsCytoskeletal ProteinsHematopoietic Cell Growth FactorsProtein Tyrosine Phosphatase, Non-Receptor Type 12Protein Tyrosine PhosphatasesPstpip1 protein, mousePtpn12 protein, mousePtpn12 protein, ratTyrosine

Identifiers

PMID9265651
PMCPMC2138048
OpenAlexW2163627937

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.