The BioGRID | PUBLICATION VIEW

	Proc. Natl. Acad. Sci. U.S.A. Nov (2006); 103(47):17840-5
Pmr1, a Golgi Ca2--Mn2--ATPase, is a regulator of the target of rapamycin -TOR- signaling pathway in yeast-
Devasahayam G, Ritz D, Helliwell SB, Burke DJ, Sturgill TW
Departments of Pharmacology, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA-
Abstract: The rapamycin-FKBP12 complex inhibits target of rapamycin -TOR- kinase in TORC1- We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2--Mn2- -ATPase- Deleting PMR1 in two genetic backgrounds confers rapamycin resistance- Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR- Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted- Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced- These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1- Together, our results establish that Pmr1-dependent Ca2- and-or Mn2- ion homeostasis is necessary for TOR signaling-
[PUBMED: 17095607]