Ubiquitin Trafficking to the Lysosome: Keeping the House Tidy and Getting Rid of Unwanted Guests

Georgiana E. Purdy and David G. Russell

volume 3 | issue 4

July/August 2007
Pages: 399 - 401

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:

Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

Bacterial killing by autophagic delivery to the lysosomal compartment has been shown for Mycobacteria, Streptococcus, Shigella, Legionella and Salmonella, indicating an important role for this conserved trafficking pathway for the control of intracellular bacterial pathogens. In a recent study we found that solubilized lysosomes isolated from bone marrow-derived macrophages had potent antibacterial properties against M. tuberculosis and M. smegmatis that were associated with ubiquitin and ubiquitin-derived peptides. We propose that ubiquitinated proteins are delivered to the lysosomal compartment, where degradation by lysosomal proteinases generates ubiquitin-derived peptides with antimycobacterial properties. This surprising finding provokes a number of questions regarding the nature and trafficking of ubiquitin and ubiquitin-modified proteins in mammalian cells. We discuss the possible role(s) that the multivesicular body (MVB), the late endosome and the autophagosome may play in trafficking of ubiquitinated proteins to the lysosome.

Addendum to:
Lysosomal Killing of Mycobacterium Mediated by Ubiquitin-Derived Peptides is Enhanced by Autophagy
S. Alonso, K. Pethe, D.G. Russell and G.E. Purdy
Proc Natl Acad Sci USA 2007; 104:6031-6

Authors

Georgiana E. Purdy

Cornell University

David G. Russell

Cornell University

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: