Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0019720
Title: Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination
Authors: Chew, K.C.M.
Matsuda, N.
Saisho, K.
Lim, G.G.Y.
Chai, C. 
Tan, H.-M.
Tanaka, K.
Lim, K.-L. 
Issue Date: 2011
Citation: Chew, K.C.M., Matsuda, N., Saisho, K., Lim, G.G.Y., Chai, C., Tan, H.-M., Tanaka, K., Lim, K.-L. (2011). Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination. PLoS ONE 6 (5) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0019720
Abstract: Background: Mutations in the parkin gene, which encodes a ubiquitin ligase (E3), are a major cause of autosomal recessive parkinsonism. Although parkin-mediated ubiquitination was initially linked to protein degradation, accumulating evidence suggests that the enzyme is capable of catalyzing multiple forms of ubiquitin modifications including monoubiquitination, K48- and K63-linked polyubiquitination. In this study, we sought to understand how a single enzyme could exhibit such multifunctional catalytic properties. Methods and Findings: By means of in vitro ubiquitination assays coupled with mass spectrometry analysis, we were surprised to find that parkin is apparently capable of mediating E2-independent protein ubiquitination in vitro, an unprecedented activity exhibited by an E3 member. Interestingly, whereas full length parkin catalyzes solely monoubiquitination regardless of the presence or absence of E2, a truncated parkin mutant containing only the catalytic moiety supports both E2-independent and E2-dependent assembly of ubiquitin chains. Conclusions: Our results here suggest a complex regulation of parkin's activity and may help to explain how a single enzyme like parkin could mediate diverse forms of ubiquitination. © 2011 Chew et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/109508
ISSN: 19326203
DOI: 10.1371/journal.pone.0019720
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