Evidence map›Paper›PMID 28003363›Full record

ArticleThe Journal of biological chemistry2017

Nuclear Localization of Integrin Cytoplasmic Domain-associated Protein-1 (ICAP1) Influences β1 Integrin Activation and Recruits Krev/Interaction Trapped-1 (KRIT1) to the Nucleus.

Kyle M Draheim, Clotilde Huet-Calderwood, Bertrand Simon, David A Calderwood

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Working a second job: Cell adhesion proteins that moonlight in the nucleus.Frontiers in cell and developmental biology · 2023
    Review
  5. ICAP-1 loss impairs CD8European journal of immunology · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  12. Article
  13. Review
  14. Review
  15. 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 1 institution in 1 country.

Kyle M DraheimFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520.
Clotilde Huet-CalderwoodFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520.
Bertrand SimonFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520.
David A CalderwoodFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520; the Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520. Electronic address: david.calderwood@yale.edu.
Yale University · US

Funding

Molecular assembly and regulation of the cerebral cavernous malformation complexR01NS085078 · NINDS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2013 to 2017
$1.8M
Determining the Functional Significance of the CCM complexF32HL127948 · NHLBI · YALE UNIVERSITY · PI DRAHEIM, KYLE MARGARET · 2015 to 2016
$120k
NHLBI NIH HHS F32 HL127948NINDS NIH HHS R01 NS085078
6 · The paper itself

Abstract

Binding of ICAP1 (integrin cytoplasmic domain-associated protein-1) to the cytoplasmic tails of β1 integrins inhibits integrin activation. ICAP1 also binds to KRIT1 (Krev interaction trapped-1), a protein whose loss of function leads to cerebral cavernous malformation, a cerebrovascular dysplasia occurring in up to 0.5% of the population. We previously showed that KRIT1 functions as a switch for β1 integrin activation by antagonizing ICAP1-mediated inhibition of integrin activation. Here we use overexpression studies, mutagenesis, and flow cytometry to show that ICAP1 contains a functional nuclear localization signal and that nuclear localization impairs the ability of ICAP1 to suppress integrin activation. Moreover, we find that ICAP1 drives the nuclear localization of KRIT1 in a manner dependent upon a direct ICAP1/KRIT1 interaction. Thus, nuclear-cytoplasmic shuttling of ICAP1 influences both integrin activation and KRIT1 localization, presumably impacting nuclear functions of KRIT1.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingAnimalsCell NucleusCHO CellsCricetinaeCricetulusHEK293 CellsHumansIntegrin beta1Intracellular Signaling Peptides and ProteinsKRIT1 ProteinMembrane ProteinsMicrotubule-Associated ProteinsProto-Oncogene ProteinsAdaptor Proteins, Signal TransducingIntegrin beta1Intracellular Signaling Peptides and ProteinsITGB1BP1 protein, humanKRIT1 ProteinKRIT1 protein, humanMembrane ProteinsMicrotubule-Associated ProteinsProto-Oncogene Proteinscell compartmentalizationcerebral cavernous malformationICAP1 (integrin cytoplasmic domain-associated protein)integrinKRIT1 (Krev interaction trapped)protein targeting

Identifiers

PMID28003363
PMCPMC5290960
OpenAlexW2566631162

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.