Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes

Tools

Item Type:	Article
Title:	Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes
Creators Name:	Ash, M.R., Faelber, K., Kosslick, D., Albert, G.I., Roske, Y., Kofler, M., Schuemann, M., Krause, E. and Freund, C.
Abstract:	The yeast suppressor of myosin 2 protein (Smy2) interacts with mRNA-processing proteins through recognition of proline-rich sequences (PRS). Here, we describe the crystal structure of the GYF domain of Smy2 in association with a PRS from the yeast branch point binding protein (BBP/ScSF1). Complex formation requires that the beta-hairpin of the central PPGL motif of the ligand is accommodated by an extended hydrophobic cleft in the domain-a specificity feature that is maintained in the human protein GIGYF2. SILAC/MS experiments in combination with PRS site inhibition show that Smy2 associates with the Ccr4-NOT deadenylase complex, whereas GIGYF2 interacts not only with mRNA surveillance factors, but also with vesicular transport proteins and Atrophin-1. GIGYF2 is shown to associate with COPII-vesicle proteins and localize to the ER and Golgi in resting cells, whereas environmental challenge drives GIGYF2 into stress granules. The current study highlights the structural basis for PRS recognition by Smy2-type GYF domains, and implicates Smy2 and GIGYF2 in both mRNA processing and the secretory pathway.
Keywords:	RNA, CELLBIO
Source:	Structure
ISSN:	0969-2126
Publisher:	Cell Press
Volume:	18
Number:	8
Page Range:	944-954
Date:	11 August 2010
Official Publication:	https://doi.org/10.1016/j.str.2010.04.020
PubMed:	View item in PubMed

Repository Staff Only: item control page