Open AccessStructure of a 14‐3‐3σ–YAP phosphopeptide complex at 1.15 Å resolution
Author(s) -
Schumacher Benjamin,
Skwarczynska Malgorzata,
Rose Rolf,
Ottmann Christian
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110025479
Subject(s) - phosphopeptide , signal transducing adaptor protein , microbiology and biotechnology , cytoplasm , gene isoform , signal transduction , biology , phosphorylation , gene , chemistry , biochemistry
The 14‐3‐3 proteins are a class of eukaryotic acidic adapter proteins, with seven isoforms in humans. 14‐3‐3 proteins mediate their biological function by binding to target proteins and influencing their activity. They are involved in pivotal pathways in the cell such as signal transduction, gene expression, enzyme activation, cell division and apoptosis. The Yes‐associated protein (YAP) is a WW‐domain protein that exists in two transcript variants of 48 and 54 kDa in humans. By transducing signals from the cytoplasm to the nucleus, YAP is important for transcriptional regulation. In both variants, interaction with 14‐3‐3 proteins after phosphorylation of Ser127 is important for nucleocytoplasmic trafficking, via which the localization of YAP is controlled. In this study, 14‐3‐3σ has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14‐3‐3‐binding domain, which led to a crystal that diffracted to 1.15 Å resolution. The crystals belonged to space group C 222 1 , with unit‐cell parameters a = 82.3, b = 112.1, c = 62.9 Å.