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@ARTICLE{Braulke:277766,
author = {T. Braulke and J. E. Carette and W. Palm$^*$},
title = {{L}ysosomal enzyme trafficking: from molecular mechanisms
to human diseases.},
journal = {Trends in cell biology},
volume = {34},
number = {3},
issn = {0962-8924},
address = {Amsterdam [u.a.]},
publisher = {Elsevier Science},
reportid = {DKFZ-2023-01481},
pages = {198-210},
year = {2024},
note = {#LA:A330# / 2024 Mar;34(3):198-210},
abstract = {Lysosomes degrade and recycle macromolecules that are
delivered through the biosynthetic, endocytic, and
autophagic routes. Hydrolysis of the different classes of
macromolecules is catalyzed by about 70 soluble enzymes that
are transported from the Golgi apparatus to lysosomes in a
mannose 6-phosphate (M6P)-dependent process. The molecular
machinery that generates M6P tags for receptor-mediated
targeting of lysosomal enzymes was thought to be understood
in detail. However, recent studies on the M6P pathway have
identified a previously uncharacterized core component,
yielded structural insights in known components, and
uncovered functions in various human diseases. Here we
review molecular mechanisms of lysosomal enzyme trafficking
and discuss its relevance for rare lysosomal disorders,
cancer, and viral infection.},
subtyp = {Review Article},
keywords = {LYSET (Other) / cancer metabolism (Other) / lysosomal
enzymes (Other) / lysosomal storage disorders (Other) /
mannose 6-phosphate pathway (Other) / viral infections
(Other)},
cin = {A330},
ddc = {570},
cid = {I:(DE-He78)A330-20160331},
pnm = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
pid = {G:(DE-HGF)POF4-311},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:37474375},
doi = {10.1016/j.tcb.2023.06.005},
url = {https://inrepo02.dkfz.de/record/277766},
}