Role of snx16 in the dynamics of tubulo-cisternal membrane domains of late endosomes

Brankatschk, Ben, Pons, Véronique, Parton, Robert G. and Gruenberg, Jean (2011) Role of snx16 in the dynamics of tubulo-cisternal membrane domains of late endosomes. PLoS One, 6 7: e21771.1-e21771.15. doi:10.1371/journal.pone.0021771

Author Brankatschk, Ben
Pons, Véronique
Parton, Robert G.
Gruenberg, Jean
Title Role of snx16 in the dynamics of tubulo-cisternal membrane domains of late endosomes
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2011-07-01
Sub-type Article (original research)
DOI 10.1371/journal.pone.0021771
Open Access Status DOI
Volume 6
Issue 7
Start page e21771.1
End page e21771.15
Total pages 15
Place of publication San Francisco, CA, United Sates
Publisher Public Library of Science
Language eng
Abstract In this paper, we report that the PX domain-containing protein SNX16, a member of the sorting nexin family, is associated with late endosome membranes. We find that SNX16 is selectively enriched on tubulo-cisternal elements of this membrane system, whose highly dynamic properties and formation depend on intact microtubules. By contrast, SNX16 was not found on vacuolar elements that typically contain LBPA, and thus presumably correspond to multivesicular endosomes. We conclude that SNX16, together with its partner phosphoinositide, define a highly dynamic subset of late endosomal membranes, supporting the notion that late endosomes are organized in distinct morphological and functional regions. Our data also indicate that SNX16 is involved in tubule formation and cholesterol transport as well as trafficking of the tetraspanin CD81, suggesting that the protein plays a role in the regulation of late endosome membrane dynamics.
Keyword Phosphatidylinositol 3-Phosphate 5-Kinase
Multivesicular Endosomes
Endocytic Pathway
Protein Rilp
Bar Domains
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article no. e21771

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
Institute for Molecular Bioscience - Publications
Centre for Microscopy and Microanalysis Publications
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Citation counts: TR Web of Science Citation Count  Cited 10 times in Thomson Reuters Web of Science Article | Citations
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