The developmental biology of Dishevelled: an enigmatic protein governing cell fate and cell polarity
Open accessAbstract
The Dishevelled protein regulates many developmental processes in animals ranging from Hydra to humans. Here, we discuss the various known signaling activities of this enigmatic protein and focus on the biological processes that Dishevelled controls. Through its many signaling activities,Dishevelled plays important roles in the embryo and the adult, ranging from cell-fate specification and cell polarity to social behavior. Dishevelled also has important roles in the governance of polarized cell divisions, in the directed migration of individual cells, and in cardiac development and neuronal structure and function.
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After binding of Wnt to the receptor complex, the signal is transduced to cytoplasmic phosphoprotein Dishevelled (Dsh/Dvl), and Dsh can directly interact with Fz.
“After binding of Wnt to the receptor complex, the signal is transduced to cytoplasmic phosphoprotein Dishevelled (Dsh/Dvl), and studies have uncovered that Dsh can directly interact with Fz.8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
Dsh is a modular protein that contains three distinct domains, a DIX, a PDZ and a DEP domain, and for canonical signaling, the DIX and PDZ domain appear to be central for mediating signaling.
“Dsh itself is a modular protein that contains three distinct domains, a DIX, a PDZ and a DEP domain and for canonical signaling, the DIX and PDZ domain appear to be central for mediating signaling.8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
The PDZ and DEP domains of Dsh are both utilized to activate two parallel pathways that activate the small GTPases Rho and Rac.
“The PDZ and DEP domains of Dsh are both utilized to activate two parallel pathways that activate the small GTPases Rho and Rac.8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
These specific domains are utilized for pathway-specific signaling.
“it appears that these specific domains are utilized for pathway specific signaling.8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
LRP-5 and LRP-6 are implicated in only the canonical pathway, while NRH1, PTK7 and ROR2 selectively transduce the non-canonical pathway.
“For example, LRP-5 and LRP-6 are implicated in only the canonical pathway,5,8 while NRH1, PTK7 and ROR2 selectively transduce the non-canonical pathway.8,113”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
Thirty or so binding partners of Dsh have been identified to date.
“Complexity of this signaling can be seen in the thirty or so binding partners identified to date”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
Co-receptors, binding partners of Dsh and/or subcellular localization of Dsh are likely the important factors that may dictate signal specificity.
“It is reasonable to propose and several studies have shown that co-receptors, binding partners of Dsh and/or subcellular localization of Dsh are likely the important factors that may dictate signal specificity.5,8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
The DEP domain of Dsh functions in non-canonical signaling.
“the DEP domain functions in non-canonical signaling.8,35”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
Components of non-canonical signaling such as Daam1, Strabismus and Prickle can bind to the PDZ domain of Dsh and function in the PCP pathway.
“The components of non-canonical signaling, such as Daam1, Strabismus and Prickle can bind to PDZ domain of Dsh and function in PCP pathway.8”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
The PDZ domain of Dsh functions in the canonical, non-canonical and Wnt/Ca2+ pathways.
“The PDZ domain of Dsh function in the canonical, non-canonical and Wnt/ Ca2+ pathway”
From Wnt signal transduction pathways (2008) · cites this paper as [8]
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- Authors
- Wallingford, J. B., & Habas, R.
- Affiliations
- The University of Texas at Austin (US)
- Rutgers Cancer Institute (US)
- Venue
- Development
- Publisher
- The Company of Biologists
- Published
- 2005-10-15
- Volume
- 132
- Issue
- 20
- Pages
- 4421-4436
- ISSN
- 0950-1991 (ISSN-L)
- 1477-9129
- OpenAlex
- W2048873522
- Cited by
- 509
- References
- 206
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 13 · 2023: 18 · 2022: 16 · 2021: 24 · 2020: 15 · 2019: 22 · 2018: 17 · 2017: 22 · 2016: 22 · 2015: 27 · 2014: 19 · 2013: 21 · 2012: 32
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Development (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- American Heart Association
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Keywords
- Dishevelled, Wnt signaling, cell fate specification, cell polarity, cell migration, heart development, neuronal development, social behavior, developmental biology
- MeSH terms
- Dishevelled Proteins, Animals, Cell Differentiation, Humans, Phosphoproteins, Signal Transduction, Cell Polarity, Cell Lineage, Adaptor Proteins, Signal Transducing, Wnt Proteins
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