ArticleJournal of molecular cell biology2014
The structure of Rap1 in complex with RIAM reveals specificity determinants and recruitment mechanism.
Article in Journal of molecular cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Investigating the effects of missense mutations on the dual Ras/Rap activation mechanism of SYNGAP1 using molecular modelling.Journal of structural biology: X · 2026Article
- The Rap1 GTPase performs two separable functions during cellularization to enable ventral furrow formation.bioRxiv : the preprint server for biology · 2026Article
- Ubiquitylation-dependent Rap2 activation regulates lamellipodia dynamics during cell migration.Journal of cell science · 2025Article
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- Platelet Membrane: An Outstanding Factor in Cancer Metastasis.Membranes · 2022Review
- Adhesion ofFrontiers in cell and developmental biology · 2022Review
- Phosphorylation of RIAM by src promotes integrin activation by unmasking the PH domain of RIAM.Structure (London, England : 1993) · 2021Article
- Distinct integrin activation pathways for effector and regulatory T cell trafficking and function.The Journal of experimental medicine · 2021Article
- Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling.Journal of cellular signaling · 2021Article
- Molecular basis for autoinhibition of RIAM regulated by FAK in integrin activation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Adhesions Assemble!-Autoinhibition as a Major Regulatory Mechanism of Integrin-Mediated Adhesion.Frontiers in molecular biosciences · 2019Review
- Volatile anesthetics affect macrophage phagocytosis.PloS one · 2019Article
- Selectins and chemokines use shared and distinct signals to activate β2 integrins in neutrophils.Blood advances · 2018Article
- Grb7 protein RA domain oligomerization.Journal of molecular recognition : JMR · 2017Article
- Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.Journal of molecular cell biology · 2017Article
- Structural and mechanistic insights into the recruitment of talin by RIAM in integrin signaling.Structure (London, England : 1993) · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The small GTPase Rap1 induces integrin activation via an inside-out signaling pathway mediated by the Rap1-interacting adaptor molecule (RIAM). Blocking this pathway may suppress tumor metastasis and other diseases that are related to hyperactive integrins. However, the molecular basis for the specific recognition of RIAM by Rap1 remains largely unknown. Herein we present the crystal structure of an active, GTP-bound GTPase domain of Rap1 in complex with the Ras association (RA)-pleckstrin homology (PH) structural module of RIAM at 1.65 Å. The structure reveals that the recognition of RIAM by Rap1 is governed by side-chain interactions. Several side chains are critical in determining specificity of this recognition, particularly the Lys31 residue in Rap1 that is oppositely charged compared with the Glu31/Asp31 residue in other Ras GTPases. Lys31 forms a salt bridge with RIAM residue Glu212, making it the key specificity determinant of the interaction. We also show that disruption of these interactions results in reduction of Rap1:RIAM association, leading to a loss of co-clustering and cell adhesion. Our findings elucidate the molecular mechanism by which RIAM mediates Rap1-induced integrin activation. The crystal structure also offers new insight into the structural basis for the specific recruitment of RA-PH module-containing effector proteins by their small GTPase partners.
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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.