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TitleStructure of the Human TELO2-TTI1-TTI2 Complex.
Journal, issue, pagesJ Mol Biol, Vol. 434, Issue 2, Page 167370, Year 2022
Publish dateJan 30, 2022
AuthorsYoungran Kim / Junhyeon Park / So Young Joo / Byung-Gyu Kim / Aera Jo / Hyunsook Lee / Yunje Cho /
PubMed AbstractPhosphatidylinositol 3-kinase-related protein kinases (PIKKs) play critical roles in various metabolic pathways related to cell proliferation and survival. The TELO2-TTI1-TTI2 (TTT) complex has been ...Phosphatidylinositol 3-kinase-related protein kinases (PIKKs) play critical roles in various metabolic pathways related to cell proliferation and survival. The TELO2-TTI1-TTI2 (TTT) complex has been proposed to recognize newly synthesized PIKKs and to deliver them to the R2TP complex (RUVBL1-RUVBL2-RPAP3-PIH1D1) and the heat shock protein 90 chaperone, thereby supporting their folding and assembly. Here, we determined the cryo-EM structure of the TTT complex at an average resolution of 4.2 Å. We describe the full-length structures of TTI1 and TELO2, and a partial structure of TTI2. All three proteins form elongated helical repeat structures. TTI1 provides a platform on which TELO2 and TTI2 bind to its central region and C-terminal end, respectively. The TELO2 C-terminal domain (CTD) is required for the interaction with TTI1 and recruitment of Ataxia-telangiectasia mutated (ATM). The N- and C-terminal segments of TTI1 recognize the FRAP-ATM-TRRAP (FAT) domain and the N-terminal HEAT repeats of ATM, respectively. The TELO2 CTD and TTI1 N- and C-terminal segments are required for cell survival in response to ionizing radiation.
External linksJ Mol Biol / PubMed:34838521
MethodsEM (single particle)
Resolution4.2 Å
Structure data

31454

7f4u

EMDB-31454, PDB-7f4u:
Cryo-EM structure of TELO2-TTI1-TTI2 complex
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / adaptor / TELO2 / TTI1 / TTI2

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