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Autophagy. 2010 May;6(4):550-2. doi: 10.4161/auto.6.4.11670. Epub 2010 May 16.

FYCO1: linking autophagosomes to microtubule plus end-directing molecular motors.

Author information

1
Molecular Cancer Research Group, Institute of Medical Biology, University of Tromsø, Tromsø, Norway.

Abstract

In mammalian cells, autophagosomes are transported along microtubule tracks to fuse with late endosomes or lysosomes. Autophagosomal membranes harbor the lipid phosphatidylinositol-3-phosphate (PtdIns(3)P) and phosphatidylethanolamine-conjugated ATG8/LC3/GABARAP family proteins. The small GTPase Rab7 is implicated in autophagosomal transport and fusion. We have recently reported that a previously uncharacterized protein FYVE and coiled-coil domain-containing 1 (FYCO1) functions as an adapter linking autophagosomes to microtubule plus end-directed molecular motors. FYCO1 binds to both LC3, PtdIns(3)P and Rab7, and contains a domain responsible for microtubule plus end-dependent transport. When cells are depleted for FYCO1, autophagosomes accumulate in perinuclear clusters, whereas overexpression of FYCO1 redistributes Rab7-positive vesicles to microtubule plus ends at the cell periphery. FYCO1 is likely selectively recruited to autophagosomal membranes via a mechanism involving a conformational change upon LC3-LIR interaction to expose the FYVE domain for PtdIns(3)P binding.

PMID:
20364109
DOI:
10.4161/auto.6.4.11670
[Indexed for MEDLINE]

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