Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation

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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

•: The RBR E3 ARIH1 assembles with numerous cullin-RING E3s via NEDD8 in mammalian cells
•: ARIH1 ligates ubiquitin to CRL substrates, enabling CDC34-dependent chain elongation
•: Two-step ARIH1 reactions involve multiple complementary interaction surfaces with CRLs
•: Several CRL substrates accumulate with ARIH1 dominant negative or depletion

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