Evidence map›Paper›PMID 40098186›Full record

ArticleCell communication and signaling : CCS2025

Inclusion of ΑVβ3 integrin into extracellular vesicles in a caveolin-1 tyrosine-14- phosphorylation dependent manner and subsequent transfer to recipient melanoma cells promotes migration, invasion and metastasis.

R Huilcaman, A Campos, P Contreras, L Simón, M Varas-Godoy, F Grünenwald, Baohai Shao, Jay Heinecke, L Lobos-Gonzalez, L Leyton and 1 more

Abstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. αvβ3-targeted gas vesicles for ultrasound molecular imaging of tumors.Frontiers in bioengineering and biotechnology · 2026
    Article
  5. Article
  6. Review
  7. 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

11 authors.

R Huilcaman *Cellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile.
A Campos *Cellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile.
P ContrerasCellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile.
L SimónCellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile.
M Varas-GodoyAdvanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, University of Chile, Santiago, Chile.
F GrünenwaldLaboratory of Reproductive Biology, Center for Biomedical Research, Faculty of Medicine, Universidad de Los Andes, Santiago, Chile.
Baohai ShaoDivision of Metabolism, Endocrinology and Nutrition, University of Washington, Seattle, WA, 98195- 8055, USA.
Jay HeineckeDivision of Metabolism, Endocrinology and Nutrition, University of Washington, Seattle, WA, 98195- 8055, USA.
L Lobos-GonzalezCellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile.
L LeytonCellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile. lleyton@med.uchile.cl.
A F G QuestCellular Communication Laboratory, Center for Studies on Exercise, Metabolism and Cancer (CEMC), Institute of Biomedical Sciences (ICBM), Faculty of Medicine, University of Chile, Santiago, Chile. aquest@med.uchile.cl.

Funding

FONDECYT, FONDAP, ANID/BASAL/, ANID postdoctoral fellowship award Becas Chile, ANID PhD fellowship awards FONDECYT grants 1210644 (A.F.G.Q.), 1200836, 1240888 (L.L.), 1211223 (L.L.-G.), 1190928 (M.V.G.), FONDAP grants 15130011 and 1523A0008 (A.F.G.Q., L.L., L.L.-G., M.V.G.), ANID/BASAL/FB210008 (M.V.G.), ANID postdoctoral fellowship award Becas Chile (A.C.), 3170169 (J.D.), ANID PhD fellowship awards 21130102 (AC), 21161246 (R.H.).
6 · The paper itself

Abstract

Caveolin-1 (CAV1) is a membrane protein that promotes migration, invasion and metastasis of cancer cells when phosphorylated on tyrosine-14 (Y14) by a cell intrinsic mechanism involving the activation of a novel Rab5-Rac1 signaling axis. Moreover, CAV1 expressed in aggressive cancer cells is included into extracellular vesicles (EVs) and such EVs increase the metastatic potential of recipient lower grade cancer cells. However, the relevance of CAV1 Y14 phosphorylation in these extrinsic EV-stimulated events remained to be determined. Here we used B16F10 mouse melanoma cells over-expressing wild-type CAV1, phospho-mimetic CAV1(Y14E) or phospho-null CAV1(Y14F) as models to determine how the EV protein content was affected by Y14 phosphorylation and how these EVs modulated the metastatic potential of recipient B16F10 cells lacking CAV1. EVs from B16F10 cells over-expressing wild-type and CAV1(Y14/E) contain CAV1, and other proteins linked to signaling pathways associated with cell adhesion and migration. CAV1 inclusion in EVs was reduced by the Y14F mutation and global protein composition was also significantly different. Moreover, CAV1 wild-type and CAV1(Y14E) EVs promoted migration, as well as invasion of cells lacking CAV1 [B16F10(Mock) cells]. In addition, β3 integrin was transferred via CAV1(Y14E) EVs to B16F10 (Mock) cells, and treatment with such EVs promoted metastasis of recipient B16F10(Mock) cells. Finally, CAV1(Y14E) EV-enhanced migration, invasion and metastasis of recipient cells was blocked by anti-αVβ3 antibodies. In conclusion, CAV1 phosphorylated on Y14 not only intrinsically promotes migration, invasion and metastasis of cells expressing the protein (in cis), but also favors the inclusion of CAV1 into EVs, as well as the extrinsic acquisition of malignant traits in recipient cells, through integrin transfer (in trans).

Indexed as

Caveolin 1Cell MovementExtracellular VesiclesIntegrin alphaVbeta3MelanomaTyrosineAnimalsCell Line, TumorHumansMelanoma, ExperimentalMiceNeoplasm InvasivenessNeoplasm MetastasisPhosphorylationCaveolin 1Integrin alphaVbeta3TyrosineB16F10 cellsCancer malignancyCaveolin-1ExosomesIntegrin transfer

Identifiers

PMID40098186
PMCPMC11912626

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.