Title: Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network
Authors : Rohrer, Jack
Kornfeld, Rosalind
Published in : Molecular Biology of the Cell
Volume(Issue) : 12
Issue : 6
Pages : 1623
Pages to: 1631
Publisher / Ed. Institution : American Society for Cell Biology
Issue Date: Jun-2001
License (according to publishing contract) : Licence according to publishing contract
Type of review: Peer review (Publication)
Language : English
Subject (DDC) : 571: Physiology and related subjects
Abstract: A crucial step in lysosomal biogenesis is catalyzed by "uncovering" enzyme (UCE), which removes a covering N-acetylglucosamine from the mannose 6-phosphate (Man-6-P) recognition marker on lysosomal hydrolases. This study shows that UCE resides in the trans-Golgi network (TGN) and cycles between the TGN and plasma membrane. The cytosolic domain of UCE contains two potential endocytosis motifs: (488)YHPL and C-terminal (511)NPFKD. YHPL is shown to be the more potent of the two in retrieval of UCE from the plasma membrane. A green-fluorescent protein-UCE transmembrane-cytosolic domain fusion protein colocalizes with TGN 46, as does endogenous UCE in HeLa cells, showing that the transmembrane and cytosolic domains determine intracellular location. These data imply that the Man-6-P recognition marker is formed in the TGN, the compartment where Man-6-P receptors bind cargo and are packaged into clathrin-coated vesicles.
Departement: Life Sciences und Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Publication type: Article in scientific Journal
DOI : 10.1091/mbc.12.6.1623
ISSN: 1939-4586
URI: https://digitalcollection.zhaw.ch/handle/11475/6801
Appears in Collections:Publikationen Life Sciences und Facility Management

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.