Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation
In: Journal of Cell Biology, Jg. 191 (2010) ; Nr. 3, S. 615-629
Zeitschriftenaufsatz / Fach: Biologie
Fakultät für Biologie » Chemische Biologie
5Caveolae are long-lived plasma membrane micro domains composed of caveolins, cams, 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 map 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 or ganelles 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
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