Evidence map›Paper›PMID 28537552›Full record

ArticleeLife2017

Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex.

Guijun Shang, Chad A Brautigam, Rui Chen, Defen Lu, Jesús Torres-Vázquez, Xuewu Zhang

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Megalin: from structure to function.Nature reviews. Nephrology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. A Genetic Polymorphism in theFrontiers in genetics · 2022
    Article
  19. A review of the mechanisms underlying the role of theFrontiers in synaptic neuroscience · 2022
    Review
  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

6 authors at 1 institution in 1 country.

Guijun ShangDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.
Chad A BrautigamDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.
Rui ChenDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.
Defen LuDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, United States.
Jesús Torres-VázquezDepartment of Cell Biology, Skirball Institute of Biomolecular Medicine, New York, United States.
Xuewu ZhangDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-3634-6711
The University of Texas Southwestern Medical Center · US

Funding

Signaling and Regulation Mechanisms of PlexinR01GM088197 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ZHANG, XUEWU · 2009 to 2017
$2.8M
Molecular Regulation of Vascular Sprout FormationR01HL133687 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI TORRES-VÁZQUEZ, JESÚS · 2016 to 2019
$2.4M
NHLBI NIH HHS R01 HL133687NIGMS NIH HHS R01 GM088197
6 · The paper itself

Abstract

The GIPC family adaptor proteins mediate endocytosis by tethering cargo proteins to the myosin VI motor. The structural mechanisms for the GIPC/cargo and GIPC/myosin VI interactions remained unclear. PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development, is a cargo of GIPCs. GIPC-mediated endocytic trafficking regulates PlexinD1 signaling. Here, we unravel the mechanisms of the interactions among PlexinD1, GIPCs and myosin VI by a series of crystal structures of these proteins in apo or bound states. GIPC1 forms a domain-swapped dimer in an autoinhibited conformation that hinders binding of both PlexinD1 and myosin VI. PlexinD1 binding to GIPC1 releases the autoinhibition, promoting its interaction with myosin VI. GIPCs and myosin VI interact through two distinct interfaces and form an open-ended alternating array. Our data support that this alternating array underlies the oligomerization of the GIPC/Myosin VI complexes in solution and cells.

Indexed as

Protein MultimerizationAdaptor Proteins, Signal TransducingAnimalsCrystallography, X-RayIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMiceModels, MolecularMyosin Heavy ChainsNerve Tissue ProteinsProtein BindingProtein ConformationAdaptor Proteins, Signal TransducingGipc1 protein, mouseIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMyosin Heavy Chainsmyosin VINerve Tissue ProteinsPlxnd1 protein, mouseautoinhibitionbiophysicsdimerizationGIPCmousemyosin VIoligomerizationPlexinstructural biology

Identifiers

PMID28537552
PMCPMC5461112
OpenAlexW2620106353

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.