Structures of Ras superfamily effector complexes: What have we learnt in two decades?

• Published in: Critical reviews in biochemistry and molecular biology Vol. 50; no. 2; pp. 85 - 133
• Main Authors: Mott, Helen R., Owen, Darerca
• Format: Journal Article
• Language: English
• Published: England Informa Healthcare USA, Inc 01.03.2015; Informa Healthcare
• Subjects: Amino Acid Sequence - genetics; Arf; GTPase; Monomeric GTP-Binding Proteins - chemistry; Monomeric GTP-Binding Proteins - classification; Monomeric GTP-Binding Proteins - genetics; Multiprotein Complexes - chemistry; Multiprotein Complexes - genetics; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Rab; Ran; Ras; ras Proteins - chemistry; ras Proteins - classification; ras Proteins - genetics; Rho; Signal Transduction; small G protein; Rab; Arf; small G protein; Ras; Rho; GTPase; Ran
• ISSN: 1040-9238; 1549-7798
• DOI: 10.3109/10409238.2014.999191

Abstract The Ras superfamily small G proteins are master regulators of a diverse range of cellular processes and act via downstream effector molecules. The first structure of a small G protein-effector complex, that of Rap1A with c-Raf1, was published 20 years ago. Since then, the structures of more than 60 small G proteins in complex with their effectors have been published. These effectors utilize a diverse array of structural motifs to interact with the G protein fold, which we have divided into four structural classes: intermolecular β-sheets, helical pairs, other interactions, and pleckstrin homology (PH) domains. These classes and their representative structures are discussed and a contact analysis of the interactions is presented, which highlights the common effector-binding regions between and within the small G protein families.