Open AccessStructures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2
Author(s) -
Pan Dongqing,
Matsuura Yoshiyuki
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112007178
Subject(s) - pleckstrin homology domain , saccharomyces cerevisiae , protein subunit , yeast , homology (biology) , microbiology and biotechnology , biology , domain (mathematical analysis) , biochemistry , chemistry , signal transduction , amino acid , gene , mathematical analysis , mathematics
In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C‐terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma‐membrane localization of TORC2 and is essential for yeast viability. X‐ray crystal structures of the C‐terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C‐termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH‐domain structures suggests a putative binding site for phosphoinositides.