Display Settings:

Format

Send to:

Choose Destination
    Autophagy. 2009 Jan;5(1):85-7. Epub 2009 Jan 13.

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

    Source

    Department of Physiology and Cell Biology, Tokyo Medical and Dental University, Tokyo, Japan.

    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.

    PMID:
    18981720
    [PubMed - indexed for MEDLINE]
    Free full text

      Supplemental Content

      Icon for Landes Bioscience

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk