Peden, A.A. orcid.org/0000-0003-0144-7712, Oorschot, V., Hesser, B.A. et al. (3 more authors)
(2004)
Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins.
Journal of Cell Biology , 164 (7).
pp. 1065-1076.
ISSN 0021-9525
Abstract
The adaptor protein (AP) 3 adaptor complex has been implicated in the transport of lysosomal membrane proteins, but its precise site of action has remained controversial. Here, we show by immuno-electron microscopy that AP-3 is associated with budding profiles evolving from a tubular endosomal compartment that also exhibits budding profiles positive for AP-1. AP-3 colocalizes with clathrin, but to a lesser extent than does AP-1. The AP-3- and AP-1-bearing tubular compartments contain endocytosed transferrin, transferrin receptor, asialoglycoprotein receptor, and low amounts of the cation-independent mannose 6-phosphate receptor and the lysosome-associated membrane proteins (LAMPs) 1 and 2. Quantitative analysis revealed that of these distinct cargo proteins, only LAMP-1 and LAMP-2 are concentrated in the AP-3-positive membrane domains. Moreover, recycling of endocytosed LAMP-1 and CD63 back to the cell surface is greatly increased in AP-3-deficient cells. Based on these data, we propose that AP-3 defines a novel pathway by which lysosomal membrane proteins are transported from tubular sorting endosomes to lysosomes.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2004 Rockefeller University Press. Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | Adaptor Protein Complex 3; Adaptor Protein Complex beta Subunits; Animals; Cell Line; Cell Membrane; Endosomes; Kinetics; Lysosomes; Membrane Proteins; Protein Transport; Transcription Factor AP-1; Transcription Factors; trans-Golgi Network |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Biomedical Science (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 22 Feb 2017 11:46 |
Last Modified: | 22 Feb 2017 11:46 |
Published Version: | https://doi.org/10.1083/jcb.200311064 |
Status: | Published |
Publisher: | Rockefeller University Press |
Refereed: | Yes |
Identification Number: | 10.1083/jcb.200311064 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:108291 |