Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.03387
Title: VAMP4 cycles from the cell surface to the trans-Golgi network via sorting and recycling endosomes
Authors: Hoai, T
Tran, T
Zeng, Q 
Hong, W 
Keywords: chimeric protein
clathrin
enhanced green fluorescent protein
SNARE protein
unclassified drug
VAMP4 protein
VAMP5 protein
amino terminal sequence
animal cell
article
carboxy terminal sequence
cell surface
cell vacuole
controlled study
endocytosis
endosome
internalization
intracellular transport
nonhuman
priority journal
protein expression
protein function
protein localization
protein motif
protein transport
rat
signal transduction
steady state
time
trans Golgi network
Animals
Cell Line
Cell Membrane
Cercopithecus aethiops
Endocytosis
Endosomes
Golgi Apparatus
Green Fluorescent Proteins
Macrolides
Mutation
Protein Sorting Signals
Protein Transport
R-SNARE Proteins
Rats
Recombinant Fusion Proteins
Issue Date: 2007
Citation: Hoai, T, Tran, T, Zeng, Q, Hong, W (2007). VAMP4 cycles from the cell surface to the trans-Golgi network via sorting and recycling endosomes. Journal of Cell Science 120 (6) : 1028-1041. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.03387
Rights: Attribution 4.0 International
Abstract: VAMP4 is enriched in the trans-Golgi network (TGN) and functions in traffic from the early and recycling endosomes to the TGN, but its trafficking itinerary is unknown. Cells stably expressing TGN-enriched VAMP4 C-terminally-tagged with EGFP (VAMP4-EGFP) are able to internalize and transport EGFP antibody efficiently to the TGN, suggesting that VAMP4-EGFP cycles between the cell surface and the TGN. The N-terminal extension of VAMP4 endows a chimeric VAMP5 with the ability to cycle from the surface to the TGN. Detailed time-course analysis of EGFP antibody transport to the TGN as well as pharmacological and thermal perturbation experiments suggest that VAMP4-EGFP is endocytosed by clathrin-dependent pathways and is delivered to the sorting and then recycling endosomes. This is followed by a direct transport to the TGN, without going through the late endosome. The di-Leu motif of the TGN-targeting signal is important for internalization, whereas the acidic cluster is crucial for efficient delivery of internalized antibody from the endosome to the TGN. These results suggest that the TGN-targeting signal of VAMP4 mediates the efficient recycling of VAMP4 from the cell surface to the TGN via the sorting and recycling endosomes, thus conferring steady-state enrichment of VAMP4 at the TGN.
Source Title: Journal of Cell Science
URI: https://scholarbank.nus.edu.sg/handle/10635/181041
ISSN: 0021-9533
DOI: 10.1242/jcs.03387
Rights: Attribution 4.0 International
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