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

Autophagy. 2009 Jan;5(1):85-7. doi: 10.4161/auto.5.1.7180. Epub 2009 Jan 13.


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.

MeSH terms

  • Animals
  • Autophagy*
  • Autophagy-Related Protein-1 Homolog
  • Autophagy-Related Proteins
  • Carrier Proteins / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mammals / metabolism*
  • Mice
  • Microtubule-Associated Proteins / metabolism
  • Models, Biological
  • Phagosomes / metabolism
  • Protein-Serine-Threonine Kinases / metabolism*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*


  • Atg17 protein, S cerevisiae
  • Autophagy-Related Proteins
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • MAP1LC3 protein, mouse
  • Microtubule-Associated Proteins
  • Rb1cc1 protein, mouse
  • Saccharomyces cerevisiae Proteins
  • Autophagy-Related Protein-1 Homolog
  • Protein-Serine-Threonine Kinases
  • Ulk1 protein, mouse