The WAVE regulatory complex links diverse receptors to the actin cytoskeleton
Open accessAbstract
The WAVE regulatory complex (WRC) controls actin cytoskeletal dynamics throughout the cell by stimulating the actin-nucleating activity of the Arp2/3 complex at distinct membrane sites. However, the factors that recruit the WRC to specific locations remain poorly understood. Here, we have identified a large family of potential WRC ligands, consisting of ∼120 diverse membrane proteins, including protocadherins, ROBOs, netrin receptors, neuroligins, GPCRs, and channels. Structural, biochemical, and cellular studies reveal that a sequence motif that defines these ligands binds to a highly conserved interaction surface of the WRC formed by the Sra and Abi subunits. Mutating this binding surface in flies resulted in defects in actin cytoskeletal organization and egg morphology during oogenesis, leading to female sterility. Our findings directly link diverse membrane proteins to the WRC and actin cytoskeleton and have broad physiological and pathological ramifications in metazoans.
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Rac1 binds to two sites on CYFIP in the WAVE complex, leading to WAVE activation.
“Rac1 binds to two sites on CYFIP in the WAVE complex, leading to WAVE activation28,30–32.”
From The WAVE complex in developmental and adulthood brain disorders (2025) · cites this paper as [28]
The Introduction identifies Sra1 as CYFIP1 and says Rac binds Sra1 and activates the WAVE regulatory complex by releasing WAVE's inhibited VCA region. The Results also show Rac1 stimulating complex activity. Neither passage establishes the claim that Rac1 binds at two sites on CYFIP. (LLM, conf=0.87)
Experimental — accuracy not yet measuredStructural studies of the WAVE complex in vitro have used a recombinant WAVE complex containing mini-WAVE, which lacks the proline-rich region due to the disordered nature of this region and difficulty in crystallization.
“Structural studies of the WAVE complex in vitro have used a recombinant WAVE complex containing mini-WAVE21,28,30,172, which lacks the proline-rich region due to the disordered nature of this region and difficulty in crystallization21.”
From The WAVE complex in developmental and adulthood brain disorders (2025) · cites this paper as [28]
The Results section ('Crystal Structure of the WIRS/WRC Complex Reveals Binding Mechanism'; page unavailable) reports crystallizing a miniWRC that lacks WAVE’s proline-rich region. The Protein Purification section also describes the WRCs as recombinant. Our copy does not say the region was omitted because it is disordered or difficult to crystallize. (LLM, conf=0.87)
Experimental — accuracy not yet measuredDynamic control of actin polymerization is crucial for cellular migration, adhesion, division, membrane transport, and spatiotemporal coordination of signals that govern metabolism and proliferation.
“Dynamic control of actin polymerization is crucial for cellular migration, adhesion, division, membrane transport, and spatiotemporal coordination of signals that govern metabolism and proliferation [1, 2].”
From HEM1 Actin Immunodysregulatory Disorder: Genotypes, Phenotypes, and Future Directions (2022) · cites this paper as [1]
The Introduction (page unavailable) says dynamic actin rearrangements are vital to eukaryotic cells and identifies adhesion, migration, and division among the processes involving WAVE proteins. The passages do not establish the claim’s additional links to membrane transport or to spatiotemporal coordination of signals governing metabolism and proliferation. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe HEM1/2 and CYFIP1/2 subunits of the WRC are structurally homologous and form a heterodimer with a flat, polybasic surface that facilitates plasma membrane association.
“The HEM1/2 and CYFIP1/2 subunits of the WRC are structurally homologous and form a heterodimer with a flat, polybasic surface that facilitates plasma membrane association [1].”
From HEM1 Actin Immunodysregulatory Disorder: Genotypes, Phenotypes, and Future Directions (2022) · cites this paper as [1]
The Introduction (page unavailable) identifies HEM1/2 as Nap1 variants and CYFIP1/2 as Sra1 variants, and describes Sra1 and Nap1 as homologous proteins that form a dimer. The passages found do not describe that dimer as having a flat, polybasic surface that facilitates plasma membrane association; the Results instead show membrane recruitment through receptor interactions. (LLM, conf=0.86)
Experimental — accuracy not yet measuredFMRP is not only involved in translation regulation and CYFIP1 is a component of complexes that do not contain FMRP.
“These conclusions are consistent with the fact that FMRP is, indeed, not only involved in translation regulation (Maurin et al., 2014) and CYFIP1 is a component of complexes that do not contain FMRP (Abekhoukh and Bardoni, 2014; Chen et al., 2014).”
From New insights into the regulatory function of CYFIP1 in the context of WAVE- and FMRP-containing complexes (2017) · cites this paper as Chen et al., 2014
Many transmembrane cell adhesion molecules and receptors, including protocadherins, ROBOs, netrin receptors, neuroligins, GPCRs and ion channels, may recruit the WAVE complex to membranes via the interaction of CYFIP and ABI with a conserved motif called WIRS.
“In addition to RAC (or ARF) and acidic phospholipids (PIP2 or PIP3), many transmembrane cell adhesion molecules and receptors, including protocadherins, ROBOs, netrin receptors, neuroligins, GPCRs and ion channels, may recruit the WAVE complex to membranes via the interaction of CYFIP and ABI with a conserved motif called WIRS (WAVE complex interacting receptor sequence)23,28 (Fig. 2).”
From The WAVE complex in developmental and adulthood brain disorders (2025) · cites this paper as [28]
At the membrane, the WRC responds to signals from phosphatidylinositol (3,4,5)-triphosphate, ABL and CDK5 kinases, and SH3-domain containing scaffolding proteins such as IRSp53.
“At the membrane, the WRC responds to a panoply of signals from phosphatidylinositol (3,4,5)-triphosphate, Abelson (ABL) and cyclin dependent kinase 5 (CDK5) kinases, and SH3-domain containing scaffolding proteins such as IRSp53 [1].”
From HEM1 Actin Immunodysregulatory Disorder: Genotypes, Phenotypes, and Future Directions (2022) · cites this paper as [1]
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“These conclusions are consistent with the fact that FMRP is, indeed, not only involved in translation regulation (Maurin et al., 2014) and CYFIP1 is a component of complexes that do not contain FMRP (Abekhoukh and Bardoni, 2014; Chen et al., 2014).”
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- Authors
- Chen, B., Brinkmann, K., Chen, Z., Pak, C. W., Liao, Y., Shi, S., Henry, L., Grishin, N. V., Bogdan, S., & Rosen, M. K.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Münster (DE)
- Corresponding author
- Bogdan, Sven
- Rosen, Michael K.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 156
- Issue
- 1-2
- Pages
- 195-207
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4059610
- OpenAlex
- W2037936544
- Cited by
- 323
- References
- 13
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 20 · 2023: 23 · 2022: 65 · 2021: 23 · 2020: 30 · 2019: 20 · 2018: 18 · 2017: 29 · 2016: 35 · 2015: 17 · 2014: 18
- FWCI
- 16.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R01GM094575, R01GM056322)
- National Institute of Diabetes and Digestive and Kidney Diseases (F32DK091074)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Keywords
- WAVE regulatory complex, Arp2/3 complex, actin cytoskeleton, protocadherins, Robo receptors, netrin receptors, neuroligins, G protein-coupled receptors, channels, oogenesis, female sterility, Drosophila
- MeSH terms
- Amino Acid Sequence, Animals, Drosophila melanogaster, Female, Humans, Membrane Proteins, Actin Cytoskeleton, Models, Molecular, Molecular Sequence Data, Oogenesis, Sequence Alignment, Crystallography, X-Ray, Drosophila Proteins, Multiprotein Complexes, Wiskott-Aldrich Syndrome Protein Family, Actin-Related Protein 2-3 Complex
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