title: Ras Association-Domain Dimers Bring Proteins Together.
abstract: In this issue of Structure, Gingras et al. (2016) show that Ras association (RA) domains of the Rap1 and Ras interacting protein Rasip1 can form a dimer in the presence and absence of the small G protein Rap1. This provides an explanation for the observed complex formation in Rap1-mediated signaling.
authors.affiliation: Molecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, 3584 CG Utrecht, Netherlands.
authors.forename: Holger
authors.initials: H
authors.lastname: Rehmann
authors.affiliation: Molecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, 3584 CG Utrecht, Netherlands. Electronic address: J.L.Bos@umcutrecht.nl.
authors.forename: Johannes L
authors.initials: JL
authors.lastname: Bos
mesh_terms: D020559:Monomeric GTP-Binding Proteins; D015398:Signal Transduction; D020827:rap1 GTP-Binding Proteins; D018631:ras Proteins
chemical_list: D020559:Monomeric GTP-Binding Proteins; D020827:rap1 GTP-Binding Proteins; D018631:ras Proteins