ArticlePharmaceutical research2015
The cellular isopeptidase T deubiquitinating enzyme regulates Kaposi's sarcoma-associated herpesvirus K7 degradation.
Article in Pharmaceutical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
5 authors.
Funding
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Abstract
purposeTo understand the regulated degradation of KSHV K7.
methodsProteomic screen and immunofluoresence microscopy identified that K7 recruits polyubiquitin chains to membrane fractions; IP and GST pulldown verified the interaction between K7 and Iso T1; Protein stability assay and RQ-PCR demonstrated Iso T1 facilitates K7 degradation.
resultsThe K7-containing membrane fraction contains a higher level of deubiquitinating (DUB) activity and K7 interacts with a cellular DUB, isopeptidase T1 (Iso T1). Mutational analyses revealed that the ubiquitin-associated domains of Iso T1 are necessary and sufficient to bind K7. Confocal microscopy and fractionation analyses indicated that K7 increases the membrane-associated Iso T1. Furthermore, the knockdown of IsoT1 by shRNA-mediated silencing greatly increased K7 ubiquitination even when proteasome activity was inhibited by lactacystin.
conclusionsIsoT1 disassembles of free ubiquitin chains to facilitate K7 degradation.
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