Phosphorylation-Dependent Regulation of WNT/Beta-Catenin Signaling
(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.
(Less)
- author
- Shah, Kinjal
LU
and Kazi, Julhash U.
LU
- organization
- publishing date
- 2022-03-14
- 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
-
- pmid:35359365
- scopus:85127706166
- 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
- 2024-08-09 22:39:51
@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}}, }