The WASP-WAVE protein network: Connecting the membrane to the cytoskeleton.
Abstract
Wiskott-Aldrich syndrome protein (WASP) and WASP-family verprolin-homologous protein (WAVE) family proteins are scaffolds that link upstream signals to the activation of the ARP2/3 complex, leading to a burst of actin polymerization. ARP2/3-complex-mediated actin polymerization is crucial for the reorganization of the actin cytoskeleton at the cell cortex for processes such as cell movement, vesicular trafficking and pathogen infection. Large families of membrane-binding proteins were recently found to interact with WASP and WAVE family proteins, therefore providing a new layer of membrane-dependent regulation of actin polymerization.
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Abi3 is suggested to exert its function through participation in the WAVE2 complex, a regulator of cytoskeletal remodeling.
“While much remains to be discovered regarding the cellular functions of Abi3, it is suggested to exert its function through its participation in the WASP family verprolin-homologous protein-2 (WAVE2) complex, a regulator of cytoskeletal remodeling (Takenawa and Suetsugu, 2007; Moraes et al., 2017).”
From Deletion of the Alzheimer’s disease risk gene Abi3 locus results in obesity and systemic metabolic disruption in mice (2022) · cites this paper as Takenawa and Suetsugu, 2007
The main role of CYFIP1 in the WAVE regulatory complex is to maintain the complex in an inhibited state until Rac1 binds CYFIP1.
“The main role of CYFIP1 in this complex is to maintain the WAVE regulatory complex in an inhibited state until the small GTPase Rac1, once activated, binds CYFIP1.”
From The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines (2014) · cites this paper as [30]
Rac1 binding results in dissociation of CYFIP1 from the WAVE regulatory complex, allowing WAVE to activate Arp2/3 and enabling de novo F-actin assembly.
“Rac1 binding results in dissociation of CYFIP1 from the WAVE regulatory complex, allowing WAVE to activate the actin nucleator Arp2/3 and subsequently enabling de novo F-actin assembly.30,31”
From The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines (2014) · cites this paper as [30]
CYFIP1 is a critical modulator of cellular actin dynamics as part of the WAVE regulatory complex.
“One critical modulator of cellular actin dynamics is the ubiquitous heteropentameric WAVE regulatory complex consisting of the proteins WAVE, Abi, Nap1, HSPC300 and CYFIP1 (also known as SRA-1) or CYFIP2.30”
From The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines (2014) · cites this paper as [30]
CYFIP1 functions as a key, conserved regulator of actin nucleation in cells.
“In this way, CYFIP1 functions as a key, conserved regulator of actin nucleation in cells.30”
From The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines (2014) · cites this paper as [30]
CYFIP1 negatively regulates local actin filament assembly.
“CYFIP1 negatively regulates local actin filament assembly, suggesting that actin dynamics may be altered in Cyfip1+/− dendritic spines.”
From The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines (2014) · cites this paper as [30]
CYFIP1 is part of the WAVE regulatory complex, a heteropentamer containing WAVE1/2/3, ABI1/2, NCKAP1, and HPSC300.
“Furthermore, CYFIP1 is part of the Wave Regulatory Complex (WRC), a heteropentamer containing also WAVE1/2/3, ABI1/2, NCKAP1 and HPSC300 (Takenawa and Suetsugu, 2007).”
From CYFIP1 Coordinates mRNA Translation and Cytoskeleton Remodeling to Ensure Proper Dendritic Spine Formation (2013) · cites this paper as Takenawa and Suetsugu, 2007
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“While much remains to be discovered regarding the cellular functions of Abi3, it is suggested to exert its function through its participation in the WASP family verprolin-homologous protein-2 (WAVE2) complex, a regulator of cytoskeletal remodeling (Takenawa and Suetsugu, 2007; Moraes et al., 2017).”
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- Authors
- Takenawa, T., & Suetsugu, S.
- Affiliations
- Institute of Medical Science, The University of Tokyo (JP)
- Japan Science and Technology Agency (JP)
- Corresponding author
- Takenawa, Tadaomi
- ORCID
- Suetsugu, Shiro
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2007-01
- Volume
- 8
- Issue
- 1
- Pages
- 37-48
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2029022457
- Cited by
- 947
- References
- 7
- Citations by year
- 2026: 16 · 2025: 26 · 2024: 21 · 2023: 39 · 2022: 44 · 2021: 40 · 2020: 29 · 2019: 35 · 2018: 30 · 2017: 49 · 2016: 47 · 2015: 42 · 2014: 70 · 2013: 42 · 2012: 79
- FWCI
- 4.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- wasps, actin cytoskeleton, membrane deformation, membrane-binding proteins, Arp2/3 complex, actin polymerization, endocytosis, membrane protrusions, cell cortex, cell motility, vesicle trafficking, pathogen infection, protein-protein interaction network
- MeSH terms
- Animals, Cell Membrane, Cytoskeleton, Humans, Phylogeny, Pseudopodia, Wiskott-Aldrich Syndrome Protein Family, Actin-Related Protein 2-3 Complex
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