Nature Search

Publisher Correction: Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane

Si Hoon Park
Juhyun Han
Hyun Kyu Song
Amendments and CorrectionsOpen Access28 Oct 2024
Nature Structural & Molecular Biology

Volume: 31, P: 1810
Publisher Correction: Heme enables proper positioning of Drosha and DGCR8 on primary microRNAs

Alexander C. Partin
Tri D. Ngo
Yunsun Nam
Amendments and CorrectionsOpen Access18 Sept 2018
Nature Communications

Volume: 9, P: 1
Cryo-EM structure of the Hippo signaling integrator human STRIPAK

A cryo-EM structure of the striatin-interacting phosphatase and kinase (STRIPAK) complex reveals the overall architecture of this large, multisubunit assembly that broadly regulates different signaling pathways.

Byung-Cheon Jeong
Sung Jun Bae
Xuelian Luo
Research25 Feb 2021
Nature Structural & Molecular Biology

Volume: 28, P: 290-299
Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane

The authors present the full-length dimeric TRIM72 E3 ubiquitin ligase and the architecture of its high-order assembly bound to a phosphatidylserine-enriched membrane, providing insights into its role in membrane repair and ubiquitylation.

Si Hoon Park
Juhyun Han
Hyun Kyu Song
ResearchOpen Access28 Sept 2023
Nature Structural & Molecular Biology

Volume: 30, P: 1695-1706
Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases

In the N-end rule pathway, the N-terminal residue of a protein is recognized by specific E3 ligases that promote its ubiquitination and proteasomal degradation. Now the structural basis for the recognition of N-terminal basic residues by the UBR box from yeast Ubr1 is solved. Together with functional analysis, the work reveals that the residue at position 2 of the substrate may influence the binding.

Woo Suk Choi
Byung-Cheon Jeong
Hyun Kyu Song
Research12 Sept 2010
Nature Structural & Molecular Biology

Volume: 17, P: 1175-1181
Heme enables proper positioning of Drosha and DGCR8 on primary microRNAs

Drosha and DGCR8 constitute the core Microprocessor complex, which processes primary microRNAs (pri-miRs) into mature microRNAs. Here the authors show that heme is essential for the proper processing of pri-miRs by Drosha-DGCR8, and the molecular mechanism by which heme enhances processing fidelity.

Alexander C. Partin
Tri D. Ngo
Yunsun Nam
ResearchOpen Access23 Nov 2017
Nature Communications

Volume: 8, P: 1-10
MG53-induced IRS-1 ubiquitination negatively regulates skeletal myogenesis and insulin signalling

The protein MG53 is known to inhibit myogenesis. Here, Ko et al. show that MG53 is an E3 ubiquitin ligase that mediates degradation of insulin receptor substrate 1 in skeletal muscle, thereby regulating myogenesis and insulin sensitivity in vitro and in vivo.

Jae-Sung Yi
Jun Sub Park
Young-Gyu Ko
Research22 Aug 2013
Nature Communications

Volume: 4, P: 1-12
Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing

The spindle checkpoint ensures the fidelity of chromosome segregation during mitosis and meiosis. Here the authors use a combination of biochemical and structural biology approaches to show how the TRIP13 ATPase and its adaptor, p31^comet, catalyze the conversion of the checkpoint protein Mad2 between latent and active forms

Melissa L. Brulotte
Byung-Cheon Jeong
Xuelian Luo
ResearchOpen Access05 Dec 2017
Nature Communications

Volume: 8, P: 1-14

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