2026-08-29T14:07:37Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/75512024-09-27T10:08:11Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19607
Repisalud
author
Zamai, Moreno
author
Trullo, Antonio
author
Giordano, Marco
author
Corti, Valeria
author
Arza, Elvira
author
Francavilla, Chiara
author
Cavallaro, Ugo
author
Caiolfa, Valeria R
funder
Fondazione Cariplo
funder
Italian Association for Cancer Research
funder
Worldwide Cancer Research
funder
Fondazione Banca del Monte di Lombardia
funder
Fondazione IEO-CCM
funder
Ministerio de Ciencia, Innovación y Universidades (España)
funder
Fundación ProCNIC
2019-05-08T05:55:04Z
2019-05-08T05:55:04Z
2019-01-03
J Cell Sci. 2019; 132(1):jcs220624
10.1242/jcs.220624
1477-9137
0021-9533
Journal of cell science
30478195
http://hdl.handle.net/20.500.12105/7551
Both fibroblast growth factor-2 (FGF2) and neural cell adhesion molecule (NCAM) trigger FGF receptor 1 (FGFR1) signaling; however, they induce remarkably distinct receptor trafficking and cellular responses. The molecular basis of such a dichotomy and the role of distinct types of ligand-receptor interaction remain elusive. Number of molecules and brightness (N&B) analysis revealed that FGF2 and NCAM promote different FGFR1 assembly and dynamics at the plasma membrane. NCAM stimulation elicits long-lasting cycles of short-lived FGFR1 monomers and multimers, a behavior that might reflect a rapid FGFR1 internalization and recycling. FGF2, instead, induces stable dimerization at the dose that stimulates cell proliferation. Reducing the occupancy of FGFR1 in response to low FGF2 doses causes a switch towards cyclically exposed and unstable receptor dimers, consistently with previously reported biphasic response to FGF2 and with the divergent signaling elicited by different ligand concentrations. Similar instability was observed upon altering the endocytic pathway. Thus, FGF2 and NCAM induce differential FGFR1 clustering at the cell surface, which might account for the distinct intracellular fate of the receptor and, hence, for the different signaling cascades and cellular responses.
eng
FGF
FGFR1
FGFR1 clustering
FGFR1 signaling
N&B analysis
NCAM
Receptor clustering
Number and brightness analysis reveals that NCAM and FGF2 elicit different assembly and dynamics of FGFR1 in live cells
journal article
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NumberBrightnessAnalysisReveals_2019.pdf
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NumberBrightnessAnalysisReveals_2019.pdf.txt