Ras Association-Domain Dimers Bring Proteins Together

Holger Rehmann; Johannes L Bos

doi:10.1016/j.str.2016.11.010

Ras Association-Domain Dimers Bring Proteins Together

Structure. 2016 Dec 6;24(12):2039-2040. doi: 10.1016/j.str.2016.11.010.

Authors

Holger Rehmann¹, Johannes L Bos²

Affiliations

¹ Molecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, 3584 CG Utrecht, Netherlands.
² 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.

PMID: 27926831
DOI: 10.1016/j.str.2016.11.010

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.

Publication types

Comment

MeSH terms

Monomeric GTP-Binding Proteins*
Signal Transduction
rap1 GTP-Binding Proteins*
ras Proteins

Substances

Monomeric GTP-Binding Proteins
rap1 GTP-Binding Proteins
ras Proteins