Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
Abstract
Parkin is a RING-between-RING E3 ligase that functions in the covalent attachment of ubiquitin to specific substrates, and mutations in Parkin are linked to Parkinson’s disease, cancer and mycobacterial infection. The RING-between-RING family of E3 ligases are suggested to function with a canonical RING domain and a catalytic cysteine residue usually restricted to HECT E3 ligases, thus termed ‘RING/HECT hybrid’ enzymes. Here we present the 1.58 Å structure of Parkin-R0RBR, revealing the fold architecture for the four RING domains, and several unpredicted interfaces. Examination of the Parkin active site suggests a catalytic network consisting of C431 and H433. In cells, mutation of C431 eliminates Parkin-catalysed degradation of mitochondria, and capture of an ubiquitin oxyester confirms C431 as Parkin’s cellular active site. Our data confirm that Parkin is a RING/HECT hybrid, and provide the first crystal structure of an RING-between-RING E3 ligase at atomic resolution, providing insight into this disease-related protein.
- Authors:
-
- Elan Pharmaceuticals, South San Francisco, CA (United States)
- SRI International, Menlo Park, CA (United States)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI Identifier:
- 1623913
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 4; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Science & Technology - Other Topics
Citation Formats
Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T., Walker, D., Yang, Y., Regnstrom, K., Diep, L., Zhang, Z., Chiou, S., Bova, M., Artis, D. R., Yao, N., Baker, J., Yednock, T., and Johnston, J. A. Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. United States: N. p., 2013.
Web. doi:10.1038/ncomms2982.
Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T., Walker, D., Yang, Y., Regnstrom, K., Diep, L., Zhang, Z., Chiou, S., Bova, M., Artis, D. R., Yao, N., Baker, J., Yednock, T., & Johnston, J. A. Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. United States. https://doi.org/10.1038/ncomms2982
Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T., Walker, D., Yang, Y., Regnstrom, K., Diep, L., Zhang, Z., Chiou, S., Bova, M., Artis, D. R., Yao, N., Baker, J., Yednock, T., and Johnston, J. A. Mon .
"Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases". United States. https://doi.org/10.1038/ncomms2982. https://www.osti.gov/servlets/purl/1623913.
@article{osti_1623913,
title = {Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases},
author = {Riley, B. E. and Lougheed, J. C. and Callaway, K. and Velasquez, M. and Brecht, E. and Nguyen, L. and Shaler, T. and Walker, D. and Yang, Y. and Regnstrom, K. and Diep, L. and Zhang, Z. and Chiou, S. and Bova, M. and Artis, D. R. and Yao, N. and Baker, J. and Yednock, T. and Johnston, J. A.},
abstractNote = {Parkin is a RING-between-RING E3 ligase that functions in the covalent attachment of ubiquitin to specific substrates, and mutations in Parkin are linked to Parkinson’s disease, cancer and mycobacterial infection. The RING-between-RING family of E3 ligases are suggested to function with a canonical RING domain and a catalytic cysteine residue usually restricted to HECT E3 ligases, thus termed ‘RING/HECT hybrid’ enzymes. Here we present the 1.58 Å structure of Parkin-R0RBR, revealing the fold architecture for the four RING domains, and several unpredicted interfaces. Examination of the Parkin active site suggests a catalytic network consisting of C431 and H433. In cells, mutation of C431 eliminates Parkin-catalysed degradation of mitochondria, and capture of an ubiquitin oxyester confirms C431 as Parkin’s cellular active site. Our data confirm that Parkin is a RING/HECT hybrid, and provide the first crystal structure of an RING-between-RING E3 ligase at atomic resolution, providing insight into this disease-related protein.},
doi = {10.1038/ncomms2982},
journal = {Nature Communications},
number = 1,
volume = 4,
place = {United States},
year = {Mon Jun 17 00:00:00 EDT 2013},
month = {Mon Jun 17 00:00:00 EDT 2013}
}
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