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

Authors
Type
Published Article
Journal
Autophagy
1554-8635
Publisher
Landes Bioscience
Publication Date
Volume
5
Issue
1
Pages
85–87
Identifiers
PMID: 18981720
Source
Medline
License
Unknown

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.

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