The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components

Gagescu, Raluca, Demaurex, Nicolas, Parton, Robert G., Hunziker, Walter, Huber, Lukas A. and Gruenberg, Jean (2000) The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Molecular Biology of the Cell, 11 8: 2775-2791.

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ249114_OA.pdf Full text (open access) application/pdf 1.13MB 0
Author Gagescu, Raluca
Demaurex, Nicolas
Parton, Robert G.
Hunziker, Walter
Huber, Lukas A.
Gruenberg, Jean
Title The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2000-08
Sub-type Critical review of research, literature review, critical commentary
Open Access Status File (Publisher version)
Volume 11
Issue 8
Start page 2775
End page 2791
Total pages 17
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Abstract We present a biochemical and morphological characterization of recycling endosomes containing the transferrin receptor in the epithelial Madin-Darby canine kidney cell line. We find that recycling endosomes are enriched in molecules known to regulate transferrin recycling but lack proteins involved in early endosome membrane dynamics, indicating that recycling endosomes are distinct from conventional early endosomes. We also find that recycling endosomes are less acidic than early endosomes because they lack a functional vacuolar ATPase. Furthermore, we show that recycling endosomes can be reached by apically internalized tracers, confirming that the apical endocytic pathway intersects the transferrin pathway. Strikingly, recycling endosomes are enriched in the raft lipids sphingomyelin and cholesterol as well as in the raft-associated proteins caveolin-1 and flotillin-1. These observations may suggest that a lipid-based sorting mechanism operates along the Madin-Darby canine kidney recycling pathway, contributing to the maintenance of cell polarity. Altogether, our data indicate that recycling endosomes and early endosomes differ functionally and biochemically and thus that different molecular mechanisms regulate protein sorting and membrane traffic at each step of the receptor recycling pathway.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 216 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Fri, 09 Sep 2011, 20:11:54 EST by System User on behalf of Learning and Research Services (UQ Library)