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Prions prefer caveosomes

The Journal of Cell Biology
The Rockefeller University Press
Publication Date
DOI: 10.1083/jcb1624iti1
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  • Biology
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Th e Jo ur na l o f C el l B io lo gy 530 The Journal of Cell Biology | Volume 162, Number 4, 2003 In This IssueIn This Issue Prions prefer caveosomes he story of prions gets increasingly bizarre. The peculiar pathogenicity of prion protein (PrP) makes understanding and treating the resulting diseases difficult. Now, on page 703, Peters et al. provide evidence that PrP also uses an unusual endocytic pathway en route to lysosomes. The harmless version of PrP is processed and directed to caveolin-rich glycolipid rafts at the plasma membrane, although its function remains a mystery. The mis- folded pathogenic form, however, is found T PrP (small gold particles) is found in endocytic structures with caveolin-1 (large particles). in late endosomes and lysosomes. The group now shows that, unlike most internalized proteins, which use the typical clathrin- dependent endocytosis pathway, PrP finds its way to lysosomes through an endosomal compartment that lacks clathrin but contains caveolin-1. The results contrast another study that reported colocalization of PrP and clathrin in vesicles. But the cryoimmunogold EM method used by Peters et al. allows for higher resolution of the vesicles and their contents. Simian virus 40 particles were also shown to be taken in through caveolin-containing, clathrin- negative structures that are connected to an endocytic vacuole (collectively termed caveosomes). Although the PrP-containing Stop and go L1CAM mobile adhesion receptor allows a cell to migrate, whereas a stationary version of the same receptor keeps it in place, based on results from Gil et al. on page 719 . The immunoglobulin family member L1CAM promotes both growth cone extension in the developing central nervous system and cell adhesion- mediated maintenance of axon bundles in mature neurons. How the same adhesion molecule regulates these disparate functions is not clear, par

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