Next Article in Journal
Aquaporins in Brain Edema and Neuropathological Conditions
Next Article in Special Issue
Unconventional Pathways of Secretion Contribute to Inflammation
Previous Article in Journal
Monitoring the Response of Hyperbilirubinemia in the Mouse Brain by In Vivo Bioluminescence Imaging
Previous Article in Special Issue
Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2017, 18(1), 47; doi:10.3390/ijms18010047

Subcellular Trafficking of Mammalian Lysosomal Proteins: An Extended View

Physiological Chemistry Laboratory-URPhyM, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editors: Gian-Pietro Di Sansebastiano and Antonio Gaballo
Received: 30 November 2016 / Revised: 15 December 2016 / Accepted: 18 December 2016 / Published: 28 December 2016
(This article belongs to the Special Issue Unconventional Proteins and Membranes Traffic)
View Full-Text   |   Download PDF [1762 KB, uploaded 28 December 2016]   |  

Abstract

Lysosomes clear macromolecules, maintain nutrient and cholesterol homeostasis, participate in tissue repair, and in many other cellular functions. To assume these tasks, lysosomes rely on their large arsenal of acid hydrolases, transmembrane proteins and membrane-associated proteins. It is therefore imperative that, post-synthesis, these proteins are specifically recognized as lysosomal components and are correctly sorted to this organelle through the endosomes. Lysosomal transmembrane proteins contain consensus motifs in their cytosolic regions (tyrosine- or dileucine-based) that serve as sorting signals to the endosomes, whereas most lysosomal acid hydrolases acquire mannose 6-phosphate (Man-6-P) moieties that mediate binding to two membrane receptors with endosomal sorting motifs in their cytosolic tails. These tyrosine- and dileucine-based motifs are tickets for boarding in clathrin-coated carriers that transport their cargo from the trans-Golgi network and plasma membrane to the endosomes. However, increasing evidence points to additional mechanisms participating in the biogenesis of lysosomes. In some cell types, for example, there are alternatives to the Man-6-P receptors for the transport of some acid hydrolases. In addition, several “non-consensus” sorting motifs have been identified, and atypical transport routes to endolysosomes have been brought to light. These “unconventional” or “less known” transport mechanisms are the focus of this review. View Full-Text
Keywords: lysosome; trafficking; unconventional; mannose 6-phosphate; alternative receptor; sorting motif lysosome; trafficking; unconventional; mannose 6-phosphate; alternative receptor; sorting motif
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Staudt, C.; Puissant, E.; Boonen, M. Subcellular Trafficking of Mammalian Lysosomal Proteins: An Extended View. Int. J. Mol. Sci. 2017, 18, 47.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top