Evidence map›Paper›PMID 19026786›Full record

ArticleMolecular cell2008

The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch.

Kenneth D Swanson, Yong Tang, Derek F Ceccarelli, Florence Poy, Jan P Sliwa, Benjamin G Neel, Michael J Eck

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Gain-of-function mutation inbioRxiv : the preprint server for biology · 2026
    Article
  3. INTEGRIN FUNCTION IN LEUKOCYTE-MEDIATED INFLAMMATION-ACTINOPATHIES IN IMMUNE DISEASES.Transactions of the American Clinical and Climatological Association · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Skap2 is required for βThe Journal of experimental medicine · 2017
    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

7 authors at 3 institutions in 1 country.

Kenneth D SwansonCancer Biology Program, Division of Hematology-Oncology, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA.
Yong Tang
Derek F Ceccarelli
Florence Poy
Jan P Sliwa
Benjamin G Neel
Michael J Eck
Dana-Farber Cancer Institute · USBeth Israel Deaconess Medical Center · USHarvard University · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
TRAINING PROGRAM IN MOLECULAR HEMATOLOGYT32HL007623 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HANDIN, ROBERT I · 1985 to 2010
$7.0M
Signal Transduction by Non-transmembrane PTPsR37CA049152 · NCI · UNIVERSITY HEALTH NETWORK · PI NEEL, BENJAMIN G. · 2004 to 2013
$4.0M
Structural biology of kinase signaling in T-cellsR01CA080942 · NCI · DANA-FARBER CANCER INSTITUTE · PI ECK, MICHAEL J · 1999 to 2010
$2.3M
Role of Gab2 and Shp2 in Hematopoietic SignallingR01CA114945 · NCI · UNIVERSITY HEALTH NETWORK · PI NEEL, BENJAMIN G. · 2006 to 2010
$1.7M
NCI NIH HHS R01 CA080942NCI NIH HHS R01CA080942NCI NIH HHS R01 CA114945NCI NIH HHS R01CA114945NCI NIH HHS R37 CA049152NCI NIH HHS R37CA 41952NCRR NIH HHS P41 RR001646NHLBI NIH HHS 2T32 HL07623-23NHLBI NIH HHS P01 HL048675NHLBI NIH HHS P01HL048675NHLBI NIH HHS T32 HL007623
6 · The paper itself

Abstract

PH domains, by binding to phosphoinositides, often serve as membrane-targeting modules. Using crystallographic, biochemical, and cell biological approaches, we have uncovered a mechanism that the integrin-signaling adaptor Skap-hom uses to mediate cytoskeletal interactions. Skap-hom is a homodimer containing an N-terminal four-helix bundle dimerization domain, against which its two PH domains pack in a conformation incompatible with phosphoinositide binding. The isolated PH domains bind PI[3,4,5]P(3), and mutations targeting the dimerization domain or the PH domain's PI[3,4,5]P(3)-binding pocket prevent Skap-hom localization to ruffles. Targeting is retained when the PH domain is deleted or by combined mutation of the PI[3,4,5]P(3)-binding pocket and the PH/dimerization domain interface. Thus, the dimerization and PH domain form a PI[3,4,5]P(3)-responsive molecular switch that controls Skap-hom function.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsDimerizationGreen Fluorescent ProteinsMiceMice, KnockoutModels, ChemicalModels, MolecularMolecular Sequence DataPhosphatidylinositolsPoint MutationProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryAdaptor Proteins, Signal TransducingGreen Fluorescent ProteinsPhosphatidylinositols

Identifiers

PMID19026786
PMCPMC2628593
OpenAlexW2018057834

What OpenQuestion holds

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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.