ARAP1 fine-tunes F-actin polymerization level in lymphocytes through RhoA inhibition.

Yoshihiro Ueda, Naoyuki Kondo, Yuji Kamioka, Tatsuo Kinashi

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Article in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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Authors and funding

4 authors.

Yoshihiro UedaDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Hirakata, Osaka, Japan.

Naoyuki KondoDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Hirakata, Osaka, Japan.

Yuji KamiokaDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Hirakata, Osaka, Japan.

Tatsuo KinashiDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Hirakata, Osaka, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rho family of small GTPases play crucial roles in F-actin polymerization and actomyosin contractility, facilitating lymphocyte polarization, motility, and adhesion. However, the spatiotemporal cooperation of these processes remains unclear. In this study, we found that the dual GTPase-activating protein (GAP) ankyrin repeat and PH domain 1 (ARAP1) modulates RhoA activity through its Ras-association (RA) domain, which binds to Rac and Rap1 and is critical for F-actin polymerization and cell migration. ARAP1 was transiently recruited to cell protrusions following chemokine stimulation. ARAP1-deficient cells exhibited enhanced chemokine-directed migration, accompanied by increased RhoA activation and F-actin polymerization. Conversely, ARAP1 overexpression had the opposite effect and inhibited migration in a manner dependent on its RhoGAP domain. Notably, the RA domain bound Rap1 and Rac1 and was required for ARAP1-mediated RhoA inhibition. These findings indicate that ARAP1 modulates RhoA activity at Rac/Rap1-rich protrusions and fine-tunes F-actin polymerization and cell motility.

Indexed as

ActinsAdaptor Proteins, Signal TransducingGTPase-Activating ProteinsLymphocytesrhoA GTP-Binding ProteinAnimalsCell MovementHumansMicePolymerizationrac1 GTP-Binding Proteinrap1 GTP-Binding ProteinsActinsAdaptor Proteins, Signal TransducingGTPase-Activating Proteinsrac1 GTP-Binding Proteinrap1 GTP-Binding ProteinsrhoA GTP-Binding ProteinRHOA protein, humanARAP1chemokineF-actin polymerizationRA-domainRhoARhoGAP

Identifiers

PMID41488654

DOI10.3389/fimmu.2025.1591450

PMCPMC12756398

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.