Evidence map›Paper›PMID 8349730›Full record

ArticleThe Journal of cell biology1993

Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells.

M Sargiacomo, M Sudol, Z Tang, M P Lisanti

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 257 papers.

0numbers the graph read from it
0cells of the map it votes in
257citing papers in PubMed
22.2field-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

257 citing papers in PubMed, 956 citations in OpenAlex.

  1. Article
  2. The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023
    Review
  3. The role of PLVAP in endothelial cells.Cell and tissue research · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Manipulation of Host Cholesterol by Obligate Intracellular Bacteria.Frontiers in cellular and infection microbiology · 2017
    Review

197 more citing papers are in PubMed but not listed here.

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.

M SargiacomoWhitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479.
M Sudol
Z Tang
M P Lisanti
Whitehead Institute for Biomedical Research · US

Funding

STRUCTURAL AND FUNCTIONAL ANALYSIS OF YES PROTO-ONCOGENER29CA045757 · NCI · ROCKEFELLER UNIVERSITY · PI SUDOL, MARIUS · 1987 to 1991
–
NCI NIH HHS NCI CA 01605NCI NIH HHS NCI CA 45757
6 · The paper itself

Abstract

GPI-linked protein molecules become Triton-insoluble during polarized sorting to the apical cell surface of epithelial cells. These insoluble complexes, enriched in cholesterol, glycolipids, and GPI-linked proteins, have been isolated by flotation on sucrose density gradients and are thought to contain the putative GPI-sorting machinery. As the cellular origin and molecular protein components of this complex remain unknown, we have begun to characterize these low-density insoluble complexes isolated from MDCK cells. We find that these complexes, which represent 0.4-0.8% of the plasma membrane, ultrastructurally resemble caveolae and are over 150-fold enriched in a model GPI-anchored protein and caveolin, a caveolar marker protein. However, they exclude many other plasma membrane associated molecules and organelle-specific marker enzymes, suggesting that they represent microdomains of the plasma membrane. In addition to caveolin, these insoluble complexes contain a subset of hydrophobic plasma membrane proteins and cytoplasmically-oriented signaling molecules, including: (a) GTP-binding proteins--both small and heterotrimeric; (b) annex II--an apical calcium-regulated phospholipid binding protein with a demonstrated role in exocytic fusion events; (c) c-Yes--an apically localized member of the Src family of non-receptor type protein-tyrosine kinases; and (d) an unidentified serine-kinase activity. As we demonstrate that caveolin is both a transmembrane molecule and a major phospho-acceptor component of these complexes, we propose that caveolin could function as a transmembrane adaptor molecule that couples luminal GPI-linked proteins with cytoplasmically oriented signaling molecules during GPI-membrane trafficking or GPI-mediated signal transduction events. In addition, our results have implications for understanding v-Src transformation and the actions of cholera and pertussis toxins on hetero-trimeric G proteins.

Indexed as

Caveolinssrc-Family KinasesAnimalsCaveolin 1Cell FractionationCell LineCell MembraneCell PolarityDetergentsDogsFibroblastsGlycosylphosphatidylinositolsGTP-Binding ProteinsIn Vitro TechniquesMembrane GlycoproteinsMembrane ProteinsCav1 protein, ratCaveolin 1CaveolinsDetergentsGlycosylphosphatidylinositolsGTP-Binding ProteinsMembrane GlycoproteinsMembrane ProteinsPhosphoproteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-yessrc-Family Kinases

Identifiers

PMID8349730
PMCPMC2119592
OpenAlexW2064754325

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.