Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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- 作者：Daniel C. Scott1 ; 2 ; 7 ; David Y. Rhee3 ; 7 ; David M. Duda1 ; 2 ; 7 ; Ian R. Kelsall4 ; Jennifer L. Olszewski1 ; Joao A. Paulo3 ; Annemieke de Jong5 ; Huib Ovaa5 ; 6 ; Arno F. Alpi4 ; J. Wade Harper3 ; wade_harper@hms.harvard.edu" class="auth_mail" title="E-mail the corresponding author ; Brenda A. Schulman1 ; 2 ; 8 ; brenda.schulman@stjude.org" class="auth_mail" title="E-mail the corresponding author
- 刊名：Cell
- 出版年：2016
- 出版时间：25 August 2016
- 年：2016
- 卷：166
- 期：5
- 页码：1198-1214.e24
- 全文大小：12194 K
文摘
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The RBR E3 ARIH1 assembles with numerous cullin-RING E3s via NEDD8 in mammalian cells
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ARIH1 ligates ubiquitin to CRL substrates, enabling CDC34-dependent chain elongation
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Two-step ARIH1 reactions involve multiple complementary interaction surfaces with CRLs
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Several CRL substrates accumulate with ARIH1 dominant negative or depletion