Evidence map›Paper›PMID 37783654›Full record

ReviewTrends in cell biology2024

Tetraspanins: structure, dynamics, and principles of partner-protein recognition.

Katherine J Susa, Andrew C Kruse, Stephen C Blacklow

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
17.4field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Tetraspanin-8 as a Tumor-Selective Immuno-PET Target in Hepatocellular Carcinoma.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2026
    Article
  13. Article
  14. Article
  15. Review
  16. Tetraspanin TSP-12 and SUP-17/ADAM10 exhibit cell type-specific codependence for trafficking through the Golgi.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

3 authors at 2 institutions in 1 country.

Katherine J SusaDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158, USA. Electronic address: katherine.susa@ucsf.edu.
Andrew C KruseDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA. Electronic address: andrew_kruse@hms.harvard.edu.
Stephen C BlacklowDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA. Electronic address: stephen_blacklow@hms.harvard.edu.
Harvard University · USUniversity of California, San Francisco · US

Funding

Notch Signaling in CancerR35CA220340 · NCI · HARVARD MEDICAL SCHOOL · PI BLACKLOW, STEPHEN C. · 2017 to 2023
$7.1M
Structure and Function of Tetraspanin ComplexesR01AI172846 · NIAID · HARVARD MEDICAL SCHOOL · PI Stephen C. Blacklow · 2022 to 2026
$4.0M
Identifying, Characterizing, and Targeting Regulators of B Cell ActivationDP5OD036136 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Katherine Julia Susa · 2023 to 2026
$1.6M
The Molecular Mechanism of the CD19-CD81 B Cell Co-Receptor ComplexF31HL147459 · NHLBI · HARVARD UNIVERSITY · PI SUSA, KATHERINE JULIA · 2019 to 2021
$103k
NCI NIH HHS R35 CA220340NHLBI NIH HHS F31 HL147459NIAID NIH HHS R01 AI172846NIH HHS DP5 OD036136
6 · The paper itself

Abstract

Tetraspanins are a large, highly conserved family of four-pass transmembrane (TM) proteins that play critical roles in a variety of essential cellular functions, including cell migration, protein trafficking, maintenance of membrane integrity, and regulation of signal transduction. Tetraspanins carry out these biological functions primarily by interacting with partner proteins. Here, we summarize significant advances that have revealed fundamental principles underpinning structure-function relationships in tetraspanins. We first review the structural features of tetraspanin ectodomains and full-length apoproteins, and then discuss how recent structural studies of tetraspanin complexes have revealed plasticity in partner-protein recognition that enables tetraspanins to bind to remarkably different protein families, viral proteins, and antibody fragments. Finally, we discuss major questions and challenges that remain in studying tetraspanin complexes.

Indexed as

Protein BindingTetraspaninsAnimalsHumansTetraspaninsintegral membrane proteinssignaling complexessignal transductionstructural biologytetraspaninstransmembrane proteins

Identifiers

PMID37783654
PMCPMC10980598
OpenAlexW4387217594

What OpenQuestion holds

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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.