Abstract

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.

Links

Publisher Full Text

Authors

Pan D, Matsuura Y

Institution

Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.

Source

Acta crystallographica. Section F, Structural biology and crystallization communications 68:Pt 4 2012 Apr 1 pg 386-92

MeSH

Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Carrier Proteins
Humans
Models, Molecular
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Tertiary
Protein Subunits
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Alignment
Structural Homology, Protein
Transcription Factors

Pub Type(s)

Journal Article

Language

eng

PubMed ID

22505404