Role of ULK-FIP200 complex in mammalian autophagy: FIP200, a counterpart of yeast Atg17?

Taichi Hara, Noboru Mizushima

Research output: Contribution to journalArticle

78 Citations (Scopus)


The yeast serine threonine kinase Atg1 appears to be a key regulator of autophagy and its kinase activity is crucial for autophagy induction. Recent reports have indicated that a mammalian Atg1 homolog, UNC-51-like kinase (ULK) 1, is required for autophagy. We found that ULK1 localizes to the autophagic isolation membrane and its kinase activity is important for autophagy induction. Furthermore, we identified a focal adhesion kinase (FAK) family interacting protein of 200 kD (FIP200) as a ULK-interacting protein. FIP200 also localizes to the isolation membrane together with ULK. Using FIP200-deficient cells, we found that FIP200 is essential for autophagosome formation and the proper function of ULK. Here, we discuss the role of the ULK-FIP200 complex in autophagy and the possibility that FIP200 functions as a mammalian counterpart of Atg17.

Original languageEnglish
Pages (from-to)85-87
Number of pages3
Issue number1
Publication statusPublished - 2009 Jan 1
Externally publishedYes



  • Atg1
  • Atg17
  • FIP200
  • Isolation membrane
  • PAS
  • ULK1

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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