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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/ Cux transcription factor.

The subclass of cysteine proteases termed lysosomal cathepsins has long been thought to be primarily involved in end-stage protein breakdown within lysosomal compartments. Furthermore, few specific protein substrates for these proteases have been identified. We show here that cathepsin L functions in the regulation of cell cycle progression through proteolytic processing of the CDP/ Cux transcription factor. CDP/ Cux processing in situ was increased following ectopic expression of cathepsin L but was reduced in Cat L(-/-) cells. Furthermore, catalytically active cathepsin L was localized to the nucleus during the G1-S transition as detected by immunofluorescence imaging and labeling using activity-based probes. Trafficking of cathepsin L to the nucleus is accomplished through a mechanism involving translation initiation at downstream AUG sites and the synthesis of proteases that are devoid of a signal peptide. Overall, these results uncover an as yet unsuspected role for cysteine proteases in the control of cell cycle progression.[1]

References

  1. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Goulet, B., Baruch, A., Moon, N.S., Poirier, M., Sansregret, L.L., Erickson, A., Bogyo, M., Nepveu, A. Mol. Cell (2004) [Pubmed]
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