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TitleULK complex organization in autophagy by a C-shaped FIP200 N-terminal domain dimer.
Journal, issue, pagesJ Cell Biol, Vol. 219, Issue 7, Year 2020
Publish dateJul 6, 2020
AuthorsXiaoshan Shi / Adam L Yokom / Chunxin Wang / Lindsey N Young / Richard J Youle / James H Hurley /
PubMed AbstractThe autophagy-initiating human ULK complex consists of the kinase ULK1/2, FIP200, ATG13, and ATG101. Hydrogen-deuterium exchange mass spectrometry was used to map their mutual interactions. The N- ...The autophagy-initiating human ULK complex consists of the kinase ULK1/2, FIP200, ATG13, and ATG101. Hydrogen-deuterium exchange mass spectrometry was used to map their mutual interactions. The N-terminal 640 residues (NTD) of FIP200 interact with the C-terminal IDR of ATG13. Mutations in these regions abolish their interaction. Negative stain EM and multiangle light scattering showed that FIP200 is a dimer, while a single molecule each of the other subunits is present. The FIP200NTD is flexible in the absence of ATG13, but in its presence adopts the shape of the letter C ∼20 nm across. The ULK1 EAT domain interacts loosely with the NTD dimer, while the ATG13:ATG101 HORMA dimer does not contact the NTD. Cryo-EM of the NTD dimer revealed a structural similarity to the scaffold domain of TBK1, suggesting an evolutionary similarity between the autophagy-initiating TBK1 kinase and the ULK1 kinase complex.
External linksJ Cell Biol / PubMed:32516362 / PubMed Central
MethodsEM (single particle)
Resolution8.4 Å
Structure data

EMDB-21325:
Focused Classification of FIP200 NTD
Method: EM (single particle) / Resolution: 8.4 Å

Source
  • Homo sapiens (human)

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