Journal article 1158 views
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...
Published in: | Traffic |
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Published: |
2004
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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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<?xml version="1.0"?><rfc1807><datestamp>2014-09-10T14:30:44.3276647</datestamp><bib-version>v2</bib-version><id>18381</id><entry>2014-09-10</entry><title>Lysosome Associated Membrane Protein 1 (Lamp1) Traffics Directly from the TGN to Early Endosomes</title><swanseaauthors><author><sid>99bb528b2f8fb62aabbdad101d53ba96</sid><firstname>Paula</firstname><surname>Row</surname><name>Paula Row</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2014-09-10</date><deptcode>BMS</deptcode><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 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.</abstract><type>Journal Article</type><journal>Traffic</journal><volume>5</volume><journalNumber>9</journalNumber><paginationStart>685</paginationStart><paginationEnd>699</paginationEnd><publisher/><keywords>avidin, endosome, Lgp120, lysosome, TGN</keywords><publishedDay>31</publishedDay><publishedMonth>12</publishedMonth><publishedYear>2004</publishedYear><publishedDate>2004-12-31</publishedDate><doi>10.1111/j.1600-0854.2004.00212.x</doi><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</url><notes/><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><lastEdited>2014-09-10T14:30:44.3276647</lastEdited><Created>2014-09-10T14:29:44.3810269</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><firstname>Neil R.</firstname><surname>Cook</surname><order>1</order></author><author><firstname>Paula</firstname><surname>Row</surname><order>2</order></author><author><firstname>Howard W.</firstname><surname>Davidson</surname><order>3</order></author></authors><documents/><OutputDurs/></rfc1807> |
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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&t=hzwpbpou&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 |
hierarchytype |
|
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facultyofmedicinehealthandlifesciences |
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Faculty of Medicine, Health and Life Sciences |
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facultyofmedicinehealthandlifesciences |
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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&t=hzwpbpou&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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1763750647486742528 |
score |
11.029921 |