Dissecting biological activities of fibroblast growth factor receptors by the coiled-coil-mediated oligomerization of FGF1

Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and apoptosis. There are a number of regulatory mechanisms of FGFR signaling, which tightly control the specificity and duration of transmitted signal...

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Published in:International journal of biological macromolecules Vol. 180; pp. 470 - 483
Main Authors: Porebska, Natalia, Pozniak, Marta, Krzyscik, Mateusz Adam, Knapik, Agata, Czyrek, Aleksandra, Kucinska, Marika, Jastrzebski, Kamil, Zakrzewska, Malgorzata, Otlewski, Jacek, Opalinski, Lukasz
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Language:English
Published: Netherlands Elsevier B.V 01-06-2021
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Abstract Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and apoptosis. There are a number of regulatory mechanisms of FGFR signaling, which tightly control the specificity and duration of transmitted signals. The effect of the FGFRs spatial distribution in the plasma membrane on receptor-dependent functions is still largely unknown. We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Set of developed FGF1 oligomers evoked prolonged activation of FGFR1 and receptor-downstream signaling pathways, as compared to the wild type FGF1. The majority of obtained oligomeric FGF1 variants showed increased stability, enhanced mitogenic activity and largely improved internalization via FGFR1-dependent endocytosis. Importantly, FGF1 oligomers with the highest oligomeric state exhibited reduced ability to stimulate FGFR-dependent glucose uptake, while at the same time remained hyperactive in the induction of cell proliferation. Our data implicate that oligomerization of FGF1 alters the biological activity of the FGF/GFR1 signaling system. Furthermore, developed FGF1 oligomers, due to improved stability and proliferative potential, can be applied in the regenerative medicine or as drug delivery vehicles in the ADC approach against FGFR1-overproducing cancers.
AbstractList Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and apoptosis. There are a number of regulatory mechanisms of FGFR signaling, which tightly control the specificity and duration of transmitted signals. The effect of the FGFRs spatial distribution in the plasma membrane on receptor-dependent functions is still largely unknown. We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Set of developed FGF1 oligomers evoked prolonged activation of FGFR1 and receptor-downstream signaling pathways, as compared to the wild type FGF1. The majority of obtained oligomeric FGF1 variants showed increased stability, enhanced mitogenic activity and largely improved internalization via FGFR1-dependent endocytosis. Importantly, FGF1 oligomers with the highest oligomeric state exhibited reduced ability to stimulate FGFR-dependent glucose uptake, while at the same time remained hyperactive in the induction of cell proliferation. Our data implicate that oligomerization of FGF1 alters the biological activity of the FGF/GFR1 signaling system. Furthermore, developed FGF1 oligomers, due to improved stability and proliferative potential, can be applied in the regenerative medicine or as drug delivery vehicles in the ADC approach against FGFR1-overproducing cancers.
Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and apoptosis. There are a number of regulatory mechanisms of FGFR signaling, which tightly control the specificity and duration of transmitted signals. The effect of the FGFRs spatial distribution in the plasma membrane on receptor-dependent functions is still largely unknown. We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Set of developed FGF1 oligomers evoked prolonged activation of FGFR1 and receptor-downstream signaling pathways, as compared to the wild type FGF1. The majority of obtained oligomeric FGF1 variants showed increased stability, enhanced mitogenic activity and largely improved internalization via FGFR1-dependent endocytosis. Importantly, FGF1 oligomers with the highest oligomeric state exhibited reduced ability to stimulate FGFR-dependent glucose uptake, while at the same time remained hyperactive in the induction of cell proliferation. Our data implicate that oligomerization of FGF1 alters the biological activity of the FGF/GFR1 signaling system. Furthermore, developed FGF1 oligomers, due to improved stability and proliferative potential, can be applied in the regenerative medicine or as drug delivery vehicles in the ADC approach against FGFR1-overproducing cancers.
Author Jastrzebski, Kamil
Knapik, Agata
Kucinska, Marika
Otlewski, Jacek
Czyrek, Aleksandra
Porebska, Natalia
Pozniak, Marta
Opalinski, Lukasz
Zakrzewska, Malgorzata
Krzyscik, Mateusz Adam
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  givenname: Natalia
  surname: Porebska
  fullname: Porebska, Natalia
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Marta
  surname: Pozniak
  fullname: Pozniak, Marta
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Mateusz Adam
  surname: Krzyscik
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  givenname: Agata
  surname: Knapik
  fullname: Knapik, Agata
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Aleksandra
  surname: Czyrek
  fullname: Czyrek, Aleksandra
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Marika
  surname: Kucinska
  fullname: Kucinska, Marika
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Kamil
  surname: Jastrzebski
  fullname: Jastrzebski, Kamil
  organization: Laboratory of Cell Biology, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland
– sequence: 8
  givenname: Malgorzata
  surname: Zakrzewska
  fullname: Zakrzewska, Malgorzata
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Jacek
  surname: Otlewski
  fullname: Otlewski, Jacek
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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  givenname: Lukasz
  surname: Opalinski
  fullname: Opalinski, Lukasz
  email: lukasz.opalinski@uwr.edu.pl
  organization: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland
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Keywords Cell division
Signaling
Oligomerization
Protein transport
Metabolism
FGFR
Language English
License This is an open access article under the CC BY license.
Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.
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Snippet Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and...
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SubjectTerms Cell division
FGFR
Metabolism
Oligomerization
Protein transport
Signaling
Title Dissecting biological activities of fibroblast growth factor receptors by the coiled-coil-mediated oligomerization of FGF1
URI https://dx.doi.org/10.1016/j.ijbiomac.2021.03.094
https://www.ncbi.nlm.nih.gov/pubmed/33745974
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