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TitleMolecular Basis of the Rapamycin Insensitivity of Target Of Rapamycin Complex 2.
Journal, issue, pagesMol Cell, Vol. 58, Issue 6, Page 977-988, Year 2015
Publish dateJun 18, 2015
AuthorsChristl Gaubitz / Taiana M Oliveira / Manoel Prouteau / Alexander Leitner / Manikandan Karuppasamy / Georgia Konstantinidou / Delphine Rispal / Sandra Eltschinger / Graham C Robinson / Stéphane Thore / Ruedi Aebersold / Christiane Schaffitzel / Robbie Loewith /
PubMed AbstractTarget of Rapamycin (TOR) plays central roles in the regulation of eukaryote growth as the hub of two essential multiprotein complexes: TORC1, which is rapamycin-sensitive, and the lesser ...Target of Rapamycin (TOR) plays central roles in the regulation of eukaryote growth as the hub of two essential multiprotein complexes: TORC1, which is rapamycin-sensitive, and the lesser characterized TORC2, which is not. TORC2 is a key regulator of lipid biosynthesis and Akt-mediated survival signaling. In spite of its importance, its structure and the molecular basis of its rapamycin insensitivity are unknown. Using crosslinking-mass spectrometry and electron microscopy, we determined the architecture of TORC2. TORC2 displays a rhomboid shape with pseudo-2-fold symmetry and a prominent central cavity. Our data indicate that the C-terminal part of Avo3, a subunit unique to TORC2, is close to the FKBP12-rapamycin-binding domain of Tor2. Removal of this sequence generated a FKBP12-rapamycin-sensitive TORC2 variant, which provides a powerful tool for deciphering TORC2 function in vivo. Using this variant, we demonstrate a role for TORC2 in G2/M cell-cycle progression.
External linksMol Cell / PubMed:26028537
MethodsEM (single particle)
Resolution26.0 Å
Structure data

EMDB-2990:
Structure of Target Of Rapapmycin Complex 2 (TORC2) from Saccharomyces cerevisiae
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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