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Phosphorylation-Dependent Regulation of WNT/Beta-Catenin Signaling

Shah, Kinjal LU and Kazi, Julhash U. LU orcid (2022) In Frontiers in Oncology 12.
Abstract

WNT/β-catenin signaling is a highly complex pathway that plays diverse roles in various cellular processes. While WNT ligands usually signal through their dedicated Frizzled receptors, the decision to signal in a β-catenin-dependent or -independent manner rests upon the type of co-receptors used. Canonical WNT signaling is β-catenin-dependent, whereas non-canonical WNT signaling is β-catenin-independent according to the classical definition. This still holds true, albeit with some added complexity, as both the pathways seem to cross-talk with intertwined networks that involve the use of different ligands, receptors, and co-receptors. β-catenin can be directly phosphorylated by various kinases governing its participation in either... (More)

WNT/β-catenin signaling is a highly complex pathway that plays diverse roles in various cellular processes. While WNT ligands usually signal through their dedicated Frizzled receptors, the decision to signal in a β-catenin-dependent or -independent manner rests upon the type of co-receptors used. Canonical WNT signaling is β-catenin-dependent, whereas non-canonical WNT signaling is β-catenin-independent according to the classical definition. This still holds true, albeit with some added complexity, as both the pathways seem to cross-talk with intertwined networks that involve the use of different ligands, receptors, and co-receptors. β-catenin can be directly phosphorylated by various kinases governing its participation in either canonical or non-canonical pathways. Moreover, the co-activators that associate with β-catenin determine the output of the pathway in terms of induction of genes promoting proliferation or differentiation. In this review, we provide an overview of how protein phosphorylation controls WNT/β-catenin signaling, particularly in human cancer.

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author
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organization
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type
Contribution to journal
publication status
published
subject
keywords
adherens junctions, AXIN, CK1, CTNNB1, frizzled, GSK3β, β-catenin
in
Frontiers in Oncology
volume
12
article number
858782
publisher
Frontiers Media S. A.
external identifiers
  • scopus:85127706166
  • pmid:35359365
ISSN
2234-943X
DOI
10.3389/fonc.2022.858782
language
English
LU publication?
yes
id
f90edac7-a5fe-4008-b38e-8b41ca9a0cce
date added to LUP
2022-06-10 10:24:30
date last changed
2024-05-31 19:29:30
@article{f90edac7-a5fe-4008-b38e-8b41ca9a0cce,
  abstract     = {{<p>WNT/β-catenin signaling is a highly complex pathway that plays diverse roles in various cellular processes. While WNT ligands usually signal through their dedicated Frizzled receptors, the decision to signal in a β-catenin-dependent or -independent manner rests upon the type of co-receptors used. Canonical WNT signaling is β-catenin-dependent, whereas non-canonical WNT signaling is β-catenin-independent according to the classical definition. This still holds true, albeit with some added complexity, as both the pathways seem to cross-talk with intertwined networks that involve the use of different ligands, receptors, and co-receptors. β-catenin can be directly phosphorylated by various kinases governing its participation in either canonical or non-canonical pathways. Moreover, the co-activators that associate with β-catenin determine the output of the pathway in terms of induction of genes promoting proliferation or differentiation. In this review, we provide an overview of how protein phosphorylation controls WNT/β-catenin signaling, particularly in human cancer.</p>}},
  author       = {{Shah, Kinjal and Kazi, Julhash U.}},
  issn         = {{2234-943X}},
  keywords     = {{adherens junctions; AXIN; CK1; CTNNB1; frizzled; GSK3β; β-catenin}},
  language     = {{eng}},
  month        = {{03}},
  publisher    = {{Frontiers Media S. A.}},
  series       = {{Frontiers in Oncology}},
  title        = {{Phosphorylation-Dependent Regulation of WNT/Beta-Catenin Signaling}},
  url          = {{http://dx.doi.org/10.3389/fonc.2022.858782}},
  doi          = {{10.3389/fonc.2022.858782}},
  volume       = {{12}},
  year         = {{2022}},
}