Nature Search

Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

The crystal structure of the PP2A holoenzyme allows insights into assembly of the subunits, recruitment of substrate, and regulation of the enzyme by phosphorylation and methylation.

Uhn Soo Cho
Wenqing Xu
Research01 Nov 2006
Nature

Volume: 445, P: 53-57
Publisher Correction: Cryo-EM structure of the human MLL1 core complex bound to the nucleosome

Sang Ho Park
Alex Ayoub
Uhn-Soo Cho
Amendments and CorrectionsOpen Access27 Feb 2020
Nature Communications

Volume: 11, P: 1
Control of substrate access to the active site in methane monooxygenase

The crystal structure of the complex between the hydroxylase and regulatory component of soluble methane monooxygenase is presented, revealing how the latter component controls substrate access to the hydroxylase active site.

Seung Jae Lee
Michael S. McCormick
Uhn-Soo Cho
Research10 Feb 2013
Nature

Volume: 494, P: 380-384
Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains

Sestrins are conserved stress-inducible metabolic regulators implicated in the prevention of agerelated diseases. Here, Kim et al.report the crystal structure of human Sestrin2 and propose a molecular mechanism for how Sestrin2 functions to prevent ROS accumulation and inhibit mTORC1 activity.

Hanseong Kim
Sojin An
Uhn-Soo Cho
ResearchOpen Access27 Nov 2015
Nature Communications

Volume: 6, P: 1-11
Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

Regulation of the MLL family of histone H3K4 methyltransferases on the nucleosome core particle (NCP) remains largely unknown. Here the authors show that intrinsically disordered regions of ASH2L and DPY30 restrict the rotational dynamics of MLL1 on the NCP, allowing more efficient enzyme-substrate engagement and higher H3K4 trimethylation activity.

Young-Tae Lee
Alex Ayoub
Yali Dou
ResearchOpen Access19 May 2021
Nature Communications

Volume: 12, P: 1-13
Non-canonical MLL1 activity regulates centromeric phase separation and genome stability

Sha et al. show that Borealin is a non-canonical methylation substrate for MLL1 that regulates phase separation of the inner centromeric chromosome passenger complex, and dictates genome integrity and tumour development in hepatocellular carcinoma.

Liang Sha
Zi Yang
Yali Dou
Research09 Nov 2023
Nature Cell Biology

Volume: 25, P: 1637-1649
Cryo-EM structure of the human MLL1 core complex bound to the nucleosome

MLL family histone methyltransferases deposit histone H3 Lys4 mono-/di-/tri-methylation and regulate gene expression in mammals. Here the authors report the single-particle cryo-EM structure of the NCP-bound human MLL1 core complex, shedding light on how the MLL1 complex engages chromatin and how chromatin binding promotes MLL1 tri-methylation activity.

Sang Ho Park
Alex Ayoub
Uhn-Soo Cho
ResearchOpen Access05 Dec 2019
Nature Communications

Volume: 10, P: 1-13
Ndc10 is a platform for inner kinetochore assembly in budding yeast

Kinetochores assemble on centromeric DNA and link centromeres to spindle microtubules, thus allowing proper segregation during mitosis. The kinetochore subunit Ndc10 makes contacts with centromeric DNA elements, which are now directly observed in a crystal structure. Along with biochemical analyses, the work indicates that Ndc10 functions as a central organizing hub to assemble the inner kinetochore.

Uhn-Soo Cho
Stephen C Harrison
Research04 Dec 2011
Nature Structural & Molecular Biology

Volume: 19, P: 48-55
Correction: Corrigendum: Sestrin2 inhibits mTORC1 through modulation of GATOR complexes

Jeong Sig Kim
Seung-Hyun Ro
Jun Hee Lee
Amendments and CorrectionsOpen Access21 Sept 2015
Scientific Reports

Volume: 5, P: 1
Concurrent activation of growth factor and nutrient arms of mTORC1 induces oxidative liver injury

Chun-Seok Cho
Allison H. Kowalsky
Jun Hee Lee
ResearchOpen Access19 Nov 2019
Cell Discovery

Volume: 5, P: 1-18
Sestrin2 inhibits mTORC1 through modulation of GATOR complexes

Jeong Sig Kim
Seung-Hyun Ro
Jun Hee Lee
ResearchOpen Access30 Mar 2015
Scientific Reports

Volume: 5, P: 1-10

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