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

Taichi Hara, Noboru Mizushima

Research output: Contribution to journalArticle

74 Citations (Scopus)

Abstract

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
JournalAutophagy
Volume5
Issue number1
Publication statusPublished - 2009 Jan 1
Externally publishedYes

Fingerprint

Autophagy
Phosphotransferases
Yeasts
Proteins
Focal Adhesion Protein-Tyrosine Kinases
Membranes
Protein-Serine-Threonine Kinases
Protein Kinases

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Role of ULK-FIP200 complex in mammalian autophagy : FIP200, a counterpart of yeast Atg17? / Hara, Taichi; Mizushima, Noboru.

In: Autophagy, Vol. 5, No. 1, 01.01.2009, p. 85-87.

Research output: Contribution to journalArticle

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