FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport.

The Journal of Cell Biology
Serhiy PankivTerje Johansen

Abstract

Autophagy is the main eukaryotic degradation pathway for long-lived proteins, protein aggregates, and cytosolic organelles. Although the protein machinery involved in the biogenesis of autophagic vesicles is well described, very little is known about the mechanism of cytosolic transport of autophagosomes. In this study, we have identified an adaptor protein complex, formed by the two autophagic membrane-associated proteins LC3 and Rab7 and the novel FYVE and coiled-coil (CC) domain-containing protein FYCO1, that promotes microtubule (MT) plus end-directed transport of autophagic vesicles. We have characterized the LC3-, Rab7-, and phosphatidylinositol-3-phosphate-binding domains in FYCO1 and mapped part of the CC region essential for MT plus end-directed transport. We also propose a mechanism for selective autophagosomal membrane recruitment of FYCO1.

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Methods Mentioned

BETA
GTPases
affinity purification
pull-down
coimmunoprecipitation
immunoprecipitation
confocal microscopy
transfection
confocal
GTPase
pull-downs

Software Mentioned

LSM
Photoshop
ProteinLynx Global server
COILS
ImageJ MTrackJ
Mascot Sciences

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