Phosphoinositide-mediated clathrin adaptor progression at the trans-Golgi network
Author: ["Lydia Daboussi","Giancarlo Costaguta","Gregory S. Payne"]
Publication: Nature Cell Biology
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Abstract
Clathrin-coated vesicles mediate endocytosis and transport between the trans-Golgi network (TGN) and endosomes in eukaryotic cells. Clathrin adaptors play central roles in coat assembly, interacting with clathrin, cargo and membranes. Two main types of clathrin adaptor act in TGN–endosome traffic: GGA proteins and the AP-1 complex. Here we characterize the relationship between GGA proteins, AP-1 and other TGN clathrin adaptors using live-cell and super-resolution microscopy in yeast. We present evidence that GGA proteins and AP-1 are recruited sequentially in two waves of coat assembly at the TGN. Mutations that decrease phosphatidylinositol 4-phosphate (PtdIns(4)P) levels at the TGN slow or uncouple AP-1 coat assembly from GGA coat assembly. Conversely, enhanced PtdIns(4)P synthesis shortens the time between adaptor waves. Gga2p binds directly to the TGN PtdIns(4)-kinase Pik1p and contributes to Pik1p recruitment. These results identify a PtdIns(4)P-based mechanism for regulating progressive assembly of adaptor-specific clathrin coats at the TGN. GGA proteins and the AP-1 complex are clathrin adaptors that regulate trans-Golgi network (TGN)-to-endosome traffic. Payne and colleagues show that these adaptors are recruited to the TGN in sequential waves, and reveal that phosphatidylinositol-4-monophosphate (PtdIns(4)P) coordinates the temporal assembly of these adaptors.
Cite this article
Daboussi, L., Costaguta, G. & Payne, G. Phosphoinositide-mediated clathrin adaptor progression at the trans-Golgi network. Nat Cell Biol 14, 239–248 (2012). https://doi.org/10.1038/ncb2427
