The C-terminal subunit of artificially truncated human cathepsin B mediates its nuclear targeting and contributes to cell viability.

ABSTRACT:

Background

Splicing variants of human cathepsinB primary transcripts (CB(-2,3)) result in an expression product product which lacks the signal peptide and parts of the propeptide. This naturally truncated Delta51CB is thus unable to follow the regular CB processing and sorting pathway. It is addressed to the mitochondria through an activated N-terminal mitochondrial targeting signal instead. Although Delta51CB is supposed to be devoid of the typical CB enzymatic activity, it might play a role in malignancies and trigger cell death/apoptosis independent from the function of the regular enzyme. Cytoplasmic presence of the mature CB might occur as a result of lysosomal damage.

Results

We investigated such "aberrant" proteins by artificial CB-GFP chimeras covering various sequen

SUBMITTER: Bestvater F 

PROVIDER: S-EPMC1087480 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature