p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase
Open accessAbstract
Rac1 small GTPase plays pivotal roles in various cell functions such as cell morphology, cell polarity, and cell proliferation. We have previously identified IQGAP1 from bovine brain cytosol as a target for Rac1 by an affinity purification method. By using the same method, we purified a specifically Rac1-associated protein with a molecular mass of about 140 kDa (p140) from bovine brain cytosol. This protein interacted with guanosine 5'-(3-O-thio)triphosphate (GTPgammaS).glutathione S-transferase (GST)-Rac1 but not with the GDP.GST-Rac1, GTPgammaS.GST-Cdc42, or GTPgammaS.GST-RhoA. The amino acid sequences of this protein revealed that p140 is identified as a product of KIAA0068 gene. We denoted this protein as Sra-1 (Specifically Rac1-associated protein). Recombinant Sra-1 interacted with GTPgammaS.GST-Rac1 and weakly with GDP.Rac1 but not with GST-Cdc42 or GST-RhoA. The N-terminal domain of Sra-1 (1-407 amino acids) was responsible for the interaction with Rac1. Myc-tagged Sra-1 and the deletion mutant capable of interacting with Rac1, but not the mutants unable to bind Rac1, were colocalized with dominant active Rac1(Val-12) and cortical actin filament at the Rac1(Val-12)-induced membrane ruffling area in KB cells. Sra-1 was cosedimented with filamentous actin (F-actin), indicating that Sra-1 directly interacts with F-actin. These results suggest that Sra-1 is a novel and specific target for Rac1.
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GTP-Rac binds CYFIP/CYFIP1, modifying its structural conformation.
“Indeed, GTP-Rac binds CYFIP/CYFIP1, modifying its structural conformation (Kobayashi et al., 1998; De Rubeis et al., 2013)”
From New insights into the regulatory function of CYFIP1 in the context of WAVE- and FMRP-containing complexes (2017) · cites this paper as Kobayashi et al., 1998
The Abstract reports that Sra-1 binds GTPγS-loaded Rac1, supporting the binding portion of the claim. Neither the Abstract nor the Results and Discussion passages report that binding changes Sra-1’s structural conformation; the paper calls the protein Sra-1 rather than CYFIP/CYFIP1. (LLM, conf=0.86)
Experimental — accuracy not yet measuredRac1 signaling can activate the WRC through CYFIP1.
“In particular, the Rac1 signaling can activate the WRC through CYFIP1 (Chen et al., 2010, Eden et al., 2002, Kobayashi et al., 1998, Schenck et al., 2003, Steffen et al., 2004).”
From CYFIP1 Coordinates mRNA Translation and Cytoskeleton Remodeling to Ensure Proper Dendritic Spine Formation (2013) · cites this paper as Kobayashi et al., 1998
The Abstract reports that Sra-1 directly interacts with activated Rac1, and Results and Discussion links Sra-1 to Rac1-induced membrane ruffling. Our copy does not identify Sra-1 as CYFIP1 or describe activation of the WRC, so it supports the Rac1–Sra-1 connection but not the full mechanism claimed. (LLM, conf=0.88)
Experimental — accuracy not yet measuredRac1 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 [31]
The Abstract reports that activated Rac1 directly interacts with Sra-1 and identifies its N-terminal domain as responsible for binding. It does not identify Sra-1 as CYFIP or report two Rac1-binding sites, a WAVE complex, or WAVE activation; the Results and Discussion instead discuss a possible role in membrane ruffling. Page numbers were not available in our copy. (LLM, conf=0.86)
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- Authors
- Kobayashi, K., Kuroda, S., Fukata, M., Nakamura, T., Nagase, T., Nomura, N., Matsuura, Y., Yoshida-Kubomura, N., Iwamatsu, A., & Kaibuchi, K.
- Affiliations
- Nara Institute of Science and Technology (JP)
- Japan Science and Technology Agency (JP)
- Hiroshima University (JP)
- Kazusa DNA Research Institute (JP)
- National Institute of Infectious Diseases (JP)
- Kirin (Japan) (JP)
- Corresponding author
- Kaibuchi, Kozo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-01
- Volume
- 273
- Issue
- 1
- Pages
- 291-295
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2032419047
- Cited by
- 244
- References
- 32
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 4 · 2023: 4 · 2022: 7 · 2021: 4 · 2020: 10 · 2019: 5 · 2018: 6 · 2017: 9 · 2016: 6 · 2015: 6 · 2014: 9 · 2013: 8 · 2012: 10
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Mitsubishi Foundation
- Japan Society for the Promotion of Science
- 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 transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- Rac1, small GTPases, GTP binding, IQGAP1, F-actin binding, cortical actin, ruffles, cell morphology
- MeSH terms
- Amino Acid Sequence, Animals, Carrier Proteins, Cattle, Molecular Sequence Data, Recombinant Proteins, Substrate Specificity, GTP-Binding Proteins, rac GTP-Binding Proteins
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