cells
Review
Fibroblast Growth Factor Receptors (FGFRs) and Noncanonical
Partners in Cancer Signaling
Harriet R. Ferguson
1
, Michael P. Smith
1,
* and Chiara Francavilla
1,2,
*
Citation: Ferguson, H.R.; Smith,
M.P.; Francavilla, C. Fibroblast
Growth Factor Receptors (FGFRs)
and Noncanonical Partners in Cancer
Signaling. Cells 2021, 10, 1201.
https://doi.org/10.3390/cells10051201
Academic Editors: Antoni Wiedlocha
and Malgorzata Zakrzewska
Received: 15 April 2021
Accepted: 9 May 2021
Published: 14 May 2021
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4.0/).
1
Division of Molecular and Cellular Function, School of Biological Science, Faculty of Biology Medicine and
Health (FBMH), The University of Manchester, Manchester M13 9PT, UK;
harriet.ferguson-2@postgrad.manchester.ac.uk
2
Manchester Breast Centre, Manchester Cancer Research Centre, The University of Manchester,
Manchester M20 4GJ, UK
* Correspondence: michael.smith-8@manchester.ac.uk (M.P.S.); chiara.francavilla@manchester.ac.uk (C.F.)
Abstract: Increasing evidence indicates that success of targeted therapies in the treatment of cancer is
context-dependent and is influenced by a complex crosstalk between signaling pathways and between
cell types in the tumor. The Fibroblast Growth Factor (FGF)/FGF receptor (FGFR) signaling axis
highlights the importance of such context-dependent signaling in cancer. Aberrant FGFR signaling
has been characterized in almost all cancer types, most commonly non-small cell lung cancer (NSCLC),
breast cancer, glioblastoma, prostate cancer and gastrointestinal cancer. This occurs primarily through
amplification and over-expression of FGFR1 and FGFR2 resulting in ligand-independent activation.
Mutations and translocations of FGFR1-4 are also identified in cancer. Canonical FGF-FGFR signaling
is tightly regulated by ligand-receptor combinations as well as direct interactions with the FGFR
coreceptors heparan sulfate proteoglycans (HSPGs) and Klotho. Noncanonical FGFR signaling
partners have been implicated in differential regulation of FGFR signaling. FGFR directly interacts
with cell adhesion molecules (CAMs) and extracellular matrix (ECM) proteins, contributing to
invasive and migratory properties of cancer cells, whereas interactions with other receptor tyrosine
kinases (RTKs) regulate angiogenic, resistance to therapy, and metastatic potential of cancer cells.
The diversity in FGFR signaling partners supports a role for FGFR signaling in cancer, independent
of genetic aberration.
Keywords: FGFRs; FGFs; signaling; cancer; tumorigenesis; coreceptors; cell adhesion molecules;
extracellular matrix; receptor tyrosine kinase; EGFR
1. Introduction
The superfamily of Receptor Tyrosine Kinases (RTKs) comprises 20 subfamilies of
cell-surface receptors with conserved structures. Upon activation, RTKs undergo dimer-
ization, internalization and initiate large-scale tyrosine phosphorylation responses and
signaling cascades to regulate cell growth, proliferation, survival and differentiation [1].
The importance of RTKs in cancer was established with the successful introduction of
Gleevec, Herceptin and Iressa, the first RTK inhibitors to show antitumor effects approved
for clinical use in the early 2000s [2]. In tandem, the role of RTKs in relation to development,
tissue homeostasis and other diseases was a growing body of research.
Among RTKs, the family of Fibroblast Growth Factor Receptors (FGFRs) comprises
four genes that give rise to at least seven different receptor isoforms. These receptors are
differentially activated by one of the 22 Fibroblast Growth Factor (FGF) ligands with known
FGFR-binding activity, which are nearly ubiquitously expressed in all adult tissues and
play a critical role in development, tissue homeostasis and human diseases [3]. Like other
RTKs, FGFR1-4 have been implicated in cancers arising from nearly all tissue types [4].
In-line with the number of ligands and receptor variants, FGFR signaling is highly context-
specific, which is evidenced by its tumorigenic or tumor suppressor roles in different
Cells 2021, 10, 1201. https://doi.org/10.3390/cells10051201 https://www.mdpi.com/journal/cells