Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

Jeannette Kunz, Ruben Henriquez, Ulrich Schneider, Maja Deuter-Reinhard, N. Rao Movva, Michael N. Hall

Research output: Contribution to journalArticlepeer-review

687 Citations (Scopus)

Abstract

The yeast TOR2 gene encodes an essential 282 kd phosphatidylinositol (PI) 3-kinase homolog. TOR2 is related to the catalytic subunit of bovine PI 3-kinase and to yeast VPS34, a vacuolar sorting protein also shown to have PI 3-kinase activity. The immunosuppressant rapamycin most likely acts by inhibiting PI kinase activity because TOR2 mutations confer resistance to rapamycin and because a TOR1 TOR2 double disruption (TOR1 is a nonessential TOR2 homolog) confers G1 arrest, as does rapamycin. Our results further suggest that 3-phosphorylated phosphoinositides, whose physiological significance has not been determined, are an important signal in cell cycle activation. In yeast, this signal may act in a signal transduction pathway similar to the interleukin-2 signal transduction pathway in T cells.

Original languageEnglish
Pages (from-to)585-596
Number of pages12
JournalCell
Volume73
Issue number3
DOIs
Publication statusPublished - May 7 1993

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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