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Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes

Neil R. Cook, Paula Row, Howard W. Davidson

Traffic, Volume: 5, Issue: 9, Pages: 685 - 699

Swansea University Author: Paula Row

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DOI (Published version): 10.1111/j.1600-0854.2004.00212.x

Abstract

The precise trafficking routes followed by newly synthe- sized lysosomal membrane proteins after exit from the Golgi are unclear. To study these events we created a novel chimera (YAL) having a lumenal domain compris- ing two tyrosine sulfation motifs fused to avidin, and the transmembrane and cytop...

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Published in: Traffic
Published: 2004
Online Access: http://onlinelibrary.wiley.com/store/10.1111/j.1600-0854.2004.00212.x/asset/j.1600-0854.2004.00212.x.pdf?v=1&t=hzwpbpou&s=b8b7d06384e9820167203022a49642432b43aa96
URI: https://cronfa.swan.ac.uk/Record/cronfa18381
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spelling 2014-09-10T14:30:44.3276647 v2 18381 2014-09-10 Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes 99bb528b2f8fb62aabbdad101d53ba96 Paula Row Paula Row true false 2014-09-10 BMS The precise trafficking routes followed by newly synthe- sized lysosomal membrane proteins after exit from the Golgi are unclear. To study these events we created a novel chimera (YAL) having a lumenal domain compris- ing two tyrosine sulfation motifs fused to avidin, and the transmembrane and cytoplasmic domains of lysosome associated membrane protein 1 (Lamp1). The newly synthesized protein rapidly transited from the trans- Golgi Network (TGN) to lysosomes (t1/2 ~30min after a lag of 15–20 min). However, labeled chimera was captured by biotinylated probes endocytosed for only 5 min, indicat- ing that the initial site of entry into the endocytic pathway was early endosomes. Capture required export of YAL from the TGN, and endocytosis of the biotinylated reagent, and was essentially quantitative within 2h of chase, suggesting that all molecules were following an identical route. There was no evidence of YAL trafficking via the cell surface. Fusion of TGN-derived vesicles with 5min endosomes could be recapitulated in vitro, but neither late endosomes nor lysosomes could serve as acceptor compartments. This suggests that contrary to previous conclusions, most if not all newly synthesized Lamp1 traffics from the TGN to early endosomes prior to delivery to late endosomes and lysosomes. Journal Article Traffic 5 9 685 699 avidin, endosome, Lgp120, lysosome, TGN 31 12 2004 2004-12-31 10.1111/j.1600-0854.2004.00212.x http://onlinelibrary.wiley.com/store/10.1111/j.1600-0854.2004.00212.x/asset/j.1600-0854.2004.00212.x.pdf?v=1&amp;t=hzwpbpou&amp;s=b8b7d06384e9820167203022a49642432b43aa96 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2014-09-10T14:30:44.3276647 2014-09-10T14:29:44.3810269 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Neil R. Cook 1 Paula Row 2 Howard W. Davidson 3
title Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
spellingShingle Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
Paula Row
title_short Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
title_full Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
title_fullStr Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
title_full_unstemmed Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
title_sort Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes
author_id_str_mv 99bb528b2f8fb62aabbdad101d53ba96
author_id_fullname_str_mv 99bb528b2f8fb62aabbdad101d53ba96_***_Paula Row
author Paula Row
author2 Neil R. Cook
Paula Row
Howard W. Davidson
format Journal article
container_title Traffic
container_volume 5
container_issue 9
container_start_page 685
publishDate 2004
institution Swansea University
doi_str_mv 10.1111/j.1600-0854.2004.00212.x
college_str Faculty of Medicine, Health and Life Sciences
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hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
url http://onlinelibrary.wiley.com/store/10.1111/j.1600-0854.2004.00212.x/asset/j.1600-0854.2004.00212.x.pdf?v=1&amp;t=hzwpbpou&amp;s=b8b7d06384e9820167203022a49642432b43aa96
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description The precise trafficking routes followed by newly synthe- sized lysosomal membrane proteins after exit from the Golgi are unclear. To study these events we created a novel chimera (YAL) having a lumenal domain compris- ing two tyrosine sulfation motifs fused to avidin, and the transmembrane and cytoplasmic domains of lysosome associated membrane protein 1 (Lamp1). The newly synthesized protein rapidly transited from the trans- Golgi Network (TGN) to lysosomes (t1/2 ~30min after a lag of 15–20 min). However, labeled chimera was captured by biotinylated probes endocytosed for only 5 min, indicat- ing that the initial site of entry into the endocytic pathway was early endosomes. Capture required export of YAL from the TGN, and endocytosis of the biotinylated reagent, and was essentially quantitative within 2h of chase, suggesting that all molecules were following an identical route. There was no evidence of YAL trafficking via the cell surface. Fusion of TGN-derived vesicles with 5min endosomes could be recapitulated in vitro, but neither late endosomes nor lysosomes could serve as acceptor compartments. This suggests that contrary to previous conclusions, most if not all newly synthesized Lamp1 traffics from the TGN to early endosomes prior to delivery to late endosomes and lysosomes.
published_date 2004-12-31T03:21:33Z
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