Scientific Article
previous document  unige:123108  next document
add to browser collection

Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation

Hayer, Arnold
Ritz, Danilo
Engel, Sabrina
Meyer, Hemmo H
Helenius, Ari
Published in The Journal of Cell Biology. 2010, vol. 191, no. 3, p. 615-629
Abstract Caveolae are long-lived plasma membrane microdomains composed of caveolins, cavins, and a cholesterol-rich membrane. Little is known about how caveolae disassemble and how their coat components are degraded. We studied the degradation of caveolin-1 (CAV1), a major caveolar protein, in CV1 cells. CAV1 was degraded very slowly, but turnover could be accelerated by compromising caveolae assembly. Now, CAV1 became detectable in late endosomes (LE) and lysosomes where it was degraded. Targeting to the degradative pathway required ubiquitination and the endosomal sorting complex required for transport (ESCRT) machinery for inclusion into intralumenal vesicles in endosomes. A dual-tag strategy allowed us to monitor exposure of CAV1 to the acidic lumen of individual, maturing LE in living cells. Importantly, we found that "caveosomes," previously described by our group as independent organelles distinct from endosomes, actually correspond to late endosomal compartments modified by the accumulation of overexpressed CAV1 awaiting degradation. The findings led us to a revised model for endocytic trafficking of CAV1.
Keywords Caveolin 1/metabolismCell LineEndosomal Sorting Complexes Required for Transport/metabolismHeLa CellsHumansLysosomes/metabolismUbiquitinated Proteins/metabolismUbiquitination
PMID: 21041450
Full text
Article (Published version) (7.2 MB) - public document Free access
Research group Contrôle subcellulaire des récepteurs de signalisation (1005)
Project Boehringer Ingelheim Fonds PhD fellowship
(ISO format)
HAYER, Arnold et al. Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation. In: The Journal of Cell Biology, 2010, vol. 191, n° 3, p. 615-629. doi: 10.1083/jcb.201003086

175 hits



Deposited on : 2019-09-12

Export document
Format :
Citation style :