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@ARTICLE{Schubert:300227,
author = {A. Schubert$^*$ and A. Mongkolsittisilp and A. Kobitski and
M. Schulz and O. Voloshanenko$^*$ and M. Schaffrinski and N.
Winkler$^*$ and M. Nessling$^*$ and K. Richter$^*$ and D.
Kranz$^*$ and K. Nienhaus and D. Jäger and L. Trümper and
J. Büntzel and C. Binder and G. U. Nienhaus and M.
Boutros$^*$},
title = {{WNT}5a export onto extracellular vesicles studied at
single-molecule and single-vesicle resolution.},
journal = {The FEBS journal},
volume = {nn},
issn = {0014-2956},
address = {Oxford [u.a.]},
publisher = {Wiley-Blackwell},
reportid = {DKFZ-2025-00689},
pages = {nn},
year = {2025},
note = {#EA:B110#LA:B110# / epub},
abstract = {WNT signaling governs development, homeostasis, and aging
of cells and tissues, and is frequently dysregulated in
pathophysiological processes such as cancer. WNT proteins
are hydrophobic and traverse the intercellular space between
the secreting and receiving cells on various carriers,
including extracellular vesicles (EVs). Here, we address the
relevance of different EV fractions and other vehicles for
WNT5a protein, a non-canonical WNT ligand that signals
independently of beta-catenin. Its highly context-dependent
roles in cancer (either tumor-suppressive or
tumor-promoting) have been attributed to two distinct
isoforms, WNT5a Short (WNT5aS) and WNT5a Long (WNT5aL),
resulting from different signal peptide cleavage sites. To
explore possible differences in secretion and extracellular
transport, we developed fusion constructs with the
fluorescent proteins (FPs) mScarlet and mOxNeonGreen.
Functional reporter assays revealed that both WNT5a isoforms
inhibit canonical WNT signaling, and EVs produced by
WNT5a-bearing tumor cells, carrying either of the WNT5a
isoforms, induced invasiveness of the luminal A breast
cancer cell line MCF7. We used fluorescence intensity
distribution analysis (FIDA) and fluorescence correlation
spectroscopy (FCS) to characterize at single-molecule
sensitivity WNT5aL-bearing entities secreted by HEK293T
cells. Importantly, we found that most WNT5aL proteins
remained monomeric in the supernatant after
ultracentrifugation; only a minor fraction was EV-bound. We
further determined the average sizes of the EV fractions and
the average number of WNT5aL proteins per EV. Our detailed
biophysical analysis of the physical nature of the EV
populations is an important step toward understanding
context-dependent WNT cargo loading and signaling in future
studies.},
keywords = {WNT signaling (Other) / WNT transport (Other) /
extracellular vesicles (Other) / fluorescence correlation
spectroscopy (Other) / number and brightness analysis
(Other)},
cin = {B110 / W230},
ddc = {610},
cid = {I:(DE-He78)B110-20160331 / I:(DE-He78)W230-20160331},
pnm = {312 - Funktionelle und strukturelle Genomforschung
(POF4-312)},
pid = {G:(DE-HGF)POF4-312},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:40165582},
doi = {10.1111/febs.70074},
url = {https://inrepo02.dkfz.de/record/300227},
}