Scar/WAVE‐1, a Wiskott–Aldrich syndrome protein, assembles an actin‐associated multi‐kinase scaffold
Open accessAbstract
WAVE proteins are members of the Wiskott-Aldrich syndrome protein (WASP) family of scaffolding proteins that coordinate actin reorganization by coupling Rho-related small molecular weight GTPases to the mobilization of the Arp2/3 complex. We identified WAVE-1 in a screen for rat brain A kinase-anchoring proteins (AKAPs), which bind to the SH3 domain of the Abelson tyrosine kinase (Abl). Recombinant WAVE-1 interacts with cAMP-dependent protein kinase (PKA) and Abl kinases when expressed in HEK-293 cells, and both enzymes co-purify with endogenous WAVE from brain extracts. Mapping studies have defined binding sites for each kinase. Competition experiments suggest that the PKA-WAVE-1 interaction may be regulated by actin as the kinase binds to a site overlapping a verprolin homology region, which has been shown to interact with actin. Immunocytochemical analyses in Swiss 3T3 fibroblasts suggest that the WAVE-1 kinase scaffold is assembled dynamically as WAVE, PKA and Abl translocate to sites of actin reorganization in response to platelet-derived growth factor treatment. Thus, we propose a previously unrecognized function for WAVE-1 as an actin-associated scaffolding protein that recruits PKA and Abl.
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WAVE1 was identified in a screen for A kinase-anchoring proteins and was characterized as a multikinase-scaffolding complex that includes PKA or ABL.
“In addition, WAVE1 was identified in a screen for A kinase-anchoring proteins (AKAPs) and was characterized as a multikinase-scaffolding complex that includes PKA or ABL82.”
From The WAVE complex in developmental and adulthood brain disorders (2025) · cites this paper as [82]
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The WAVE complex in developmental and adulthood brain disorders
Kim, H.-G., Berdasco, C., Nairn, A. C., & Kim, Y. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01386-w · Cited by 8 · see citing works
- Authors
- Westphal, R. S., Soderling, S. H., Alto, N. M., Langeberg, L. K., & Scott, J. D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Oregon Health & Science University (US)
- Corresponding author
- Scott, John D.
- Venue
- The EMBO Journal
- Published
- 2000-09-01
- Volume
- 19
- Issue
- 17
- Pages
- 4589-4600
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC302050
- OpenAlex
- W2128331958
- Cited by
- 205
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 2 · 2019: 1 · 2017: 3 · 2016: 4 · 2015: 2 · 2014: 8 · 2013: 7 · 2012: 6
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The EMBO Journal
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (P01DK044239, DK44239)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- 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
- Keywords
- A-kinase anchoring proteins, protein kinase A, c-Abl, Arp2/3 complex, actin reorganization, platelet-derived growth factor
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Immunohistochemistry, Microfilament Proteins, Molecular Sequence Data, Precipitin Tests, Protein Binding, Recombinant Proteins, Wiskott-Aldrich Syndrome, Signal Transduction, Oncogene Proteins v-abl, 3T3 Cells, Sequence Homology, Amino Acid, Cyclic AMP-Dependent Protein Kinases, DNA Primers, Protein Isoforms, Wiskott-Aldrich Syndrome Protein Family, Mice, Rats
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