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Issue 6, 2011
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Detection of a secreted metalloprotease within the nuclei of liver cells

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Abstract

ADAMTS13 is a secreted zinc metalloprotease expressed by various cell types. Here, we investigate its cellular pathway in endogenously expressing liver cell lines and after transient transfection with ADAMTS13. Besides compartmentalizations of the cellular secretory system, we detected an appreciable level of endogenous ADAMTS13 within the nucleus. A positively charged amino acid cluster (R-Q-R-Q-R-Q-R-R) present in the ADAMTS13 propeptide may act as a nuclear localization signal (NLS). Fusing this NLS-containing region to eGFP greatly potentiated its nuclear localization. Bioinformatics analysis suggests that the ADAMTS13 CUB-2 domain has a double-stranded beta helix (DSBH) structural architecture characteristic of various proteinprotein interaction modules like nucleoplasmins, class I collagenase, tumor necrosis factor ligand superfamily, supernatant protein factor (SPF) and the B1 domain of neuropilin-2. Based on this contextual evidence and that largely conserved polar residues could be mapped on to a template CUB domain homolog, we hypothesize that a region in the ADAMTS13 CUB-2 domain with conserved polar residues might be involved in proteinprotein interaction within the nucleus.

Graphical abstract: Detection of a secreted metalloprotease within the nuclei of liver cells

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Publication details

The article was received on 29 Nov 2010, accepted on 15 Mar 2011 and first published on 11 Apr 2011


Article type: Paper
DOI: 10.1039/C0MB00303D
Citation: Mol. BioSyst., 2011,7, 2012-2018
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    Detection of a secreted metalloprotease within the nuclei of liver cells

    R. C. Hunt, S. Geetha, C. E. Allen, K. Hershko, R. Fathke, P. L. Kong, E. Plum, E. B. Struble, K. Soejima, S. Friedman, S. Garfield, S. Balaji and C. Kimchi-Sarfaty, Mol. BioSyst., 2011, 7, 2012
    DOI: 10.1039/C0MB00303D

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