Evidence map›Paper›PMID 20167601›Full record

ArticleThe Journal of biological chemistry2010

Structural basis of membrane targeting by the Dock180 family of Rho family guanine exchange factors (Rho-GEFs).

Lakshmanane Premkumar, Andrey A Bobkov, Manishha Patel, Lukasz Jaroszewski, Laurie A Bankston, Boguslaw Stec, Kristiina Vuori, Jean-Francois Côté, Robert C Liddington

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
2.6field-weighted citation impact, top 11% 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, 65 citations in OpenAlex.

  1. Structural basis for membrane-dependent positive feedback regulation of DOCK11 by activated Cdc42.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
  9. Review
  10. Dendritic cells in inborn errors of immunity.Frontiers in immunology · 2023
    Review
  11. Review
  12. DOCK4 Regulation of Rho GTPases Mediates Pulmonary Vascular Barrier Function.Arteriosclerosis, thrombosis, and vascular biology · 2022
    Article
  13. Article
  14. GPCRs thatSmall GTPases · 2022
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

9 authors at 2 institutions in 2 countries.

Lakshmanane PremkumarInfectious and Inflammatory Disease Center, Sanford-Burnham Medical Research Institute, La Jolla, California 92037, USA.
Andrey A Bobkov
Manishha Patel
Lukasz Jaroszewski
Laurie A Bankston
Boguslaw Stec
Kristiina Vuori
Jean-Francois Côté
Robert C Liddington
Sanford Burnham Prebys Medical Discovery Institute · USMontreal Clinical Research Institute · CA

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
CIHR 77591NIGMS NIH HHS U54 GM06346NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

The Dock180 family of atypical Rho family guanine nucleotide exchange factors (Rho-GEFs) regulate a variety of processes involving cellular or subcellular polarization, including cell migration and phagocytosis. Each contains a Dock homology region-1 (DHR-1) domain that is required to localize its GEF activity to a specific membrane compartment where levels of phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P(3)) are up-regulated by the local activity of PtdIns 3-kinase. Here we define the structural and energetic bases of phosphoinositide specificity by the DHR-1 domain of Dock1 (a GEF for Rac1), and show that DHR-1 utilizes a C2 domain scaffold and surface loops to create a basic pocket on its upper surface for recognition of the PtdIns(3,4,5)P(3) head group. The pocket has many of the characteristics of those observed in pleckstrin homology domains. We show that point mutations in the pocket that abolish phospholipid binding in vitro ablate the ability of Dock1 to induce cell polarization, and propose a model that brings together recent mechanistic and structural studies to rationalize the central role of DHR-1 in dynamic membrane targeting of the Rho-GEF activity of Dock180.

Indexed as

Models, MolecularAnimalsBinding SitesCytoskeletal ProteinsDrosophila melanogasterDrosophila ProteinsHumansMultigene FamilyPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesProtein Structure, SecondaryProtein Structure, Tertiaryrac GTP-Binding Proteinsrho GTP-Binding ProteinsStructural Homology, ProteinStructure-Activity RelationshipCytoskeletal ProteinsDOCK1 protein, humanDrosophila Proteinsmbc protein, Drosophilaphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol 3-KinasesPhosphatidylinositol Phosphatesrac GTP-Binding Proteinsrho GTP-Binding Proteins

Identifiers

PMID20167601
PMCPMC2857062
OpenAlexW2054082789

What OpenQuestion holds

Textmetadata
LicenceTDM
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.