A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases

How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8’s E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 th...

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Autores principales: Calabrese, Matthew F., Scott, Daniel C., Duda, David M., Grace, Christy R.R., Kurinov, Igor, Kriwacki, Richard W., Schulman, Brenda A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245743/
https://www.ncbi.nlm.nih.gov/pubmed/21765416
http://dx.doi.org/10.1038/nsmb.2086
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author Calabrese, Matthew F.
Scott, Daniel C.
Duda, David M.
Grace, Christy R.R.
Kurinov, Igor
Kriwacki, Richard W.
Schulman, Brenda A.
author_facet Calabrese, Matthew F.
Scott, Daniel C.
Duda, David M.
Grace, Christy R.R.
Kurinov, Igor
Kriwacki, Richard W.
Schulman, Brenda A.
author_sort Calabrese, Matthew F.
collection PubMed
description How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8’s E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.
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spelling pubmed-32457432012-02-01 A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases Calabrese, Matthew F. Scott, Daniel C. Duda, David M. Grace, Christy R.R. Kurinov, Igor Kriwacki, Richard W. Schulman, Brenda A. Nat Struct Mol Biol Article How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8’s E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s. 2011-07-17 /pmc/articles/PMC3245743/ /pubmed/21765416 http://dx.doi.org/10.1038/nsmb.2086 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Calabrese, Matthew F.
Scott, Daniel C.
Duda, David M.
Grace, Christy R.R.
Kurinov, Igor
Kriwacki, Richard W.
Schulman, Brenda A.
A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title_full A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title_fullStr A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title_full_unstemmed A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title_short A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
title_sort ring e3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-ring ligases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245743/
https://www.ncbi.nlm.nih.gov/pubmed/21765416
http://dx.doi.org/10.1038/nsmb.2086
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