Výsledky vyhledávání - "Frank Sicheri"

Akademický článek

A screen for MeCP2-TBL1 interaction inhibitors using a luminescence-based assay

Autor: Beatrice Alexander-Howden, Li Zhang, Almer M. van der Sloot, Sylvain Tollis, Daniel J. St-Cyr, Frank Sicheri, Adrian P. Bird, Mike Tyers, Matthew J. Lyst

Publikováno v: Scientific Reports, Vol 13, Iss 1, Pp 1-10 (2023)

Abstract Understanding the molecular pathology of neurodevelopmental disorders should aid the development of therapies for these conditions. In MeCP2 duplication syndrome (MDS)—a severe autism spectrum disorder—neuronal dysfunction is caused by i

Externí odkaz: https://doaj.org/article/6d644a3749a64fcd9972878fe0db5ac2

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Akademický článek

A substrate binding model for the KEOPS tRNA modifying complex

Autor: Jonah Beenstock, Samara Mishelle Ona, Jennifer Porat, Stephen Orlicky, Leo C. K. Wan, Derek F. Ceccarelli, Pierre Maisonneuve, Rachel K. Szilard, Zhe Yin, Dheva Setiaputra, Daniel Y. L. Mao, Morgan Khan, Shaunak Raval, David C. Schriemer, Mark A. Bayfield, Daniel Durocher, Frank Sicheri

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)

KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA c

Externí odkaz: https://doaj.org/article/7cf78e57b0794aac8b3b0de7021b5c2b

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Akademický článek

Monoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1

Autor: Salima Daou, Haithem Barbour, Oumaima Ahmed, Louis Masclef, Caroline Baril, Nadine Sen Nkwe, Daméhan Tchelougou, Maxime Uriarte, Eric Bonneil, Derek Ceccarelli, Nazar Mashtalir, Mika Tanji, Jean-Yves Masson, Pierre Thibault, Frank Sicheri, Haining Yang, Michele Carbone, Marc Therrien, El Bachir Affar

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-21 (2018)

Additional sex combs-like (ASXLs) stimulate BAP1 deubiquitinase activity to induce tumor suppression, but how these complexes work in coordination in vivo is unclear. Here, the authors show the mutually reinforcing roles of BAP1 and ASXLs such that B

Externí odkaz: https://doaj.org/article/814d9c18ef9a493e9a4123fb81cb86a6

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Akademický článek

Robust cullin-RING ligase function is established by a multiplicity of poly-ubiquitylation pathways

Autor: Spencer Hill, Kurt Reichermeier, Daniel C Scott, Lorena Samentar, Jasmin Coulombe-Huntington, Luisa Izzi, Xiaojing Tang, Rebeca Ibarra, Thierry Bertomeu, Annie Moradian, Michael J Sweredoski, Nora Caberoy, Brenda A Schulman, Frank Sicheri, Mike Tyers, Gary Kleiger

Publikováno v: eLife, Vol 8 (2019)

The cullin-RING ligases (CRLs) form the major family of E3 ubiquitin ligases. The prototypic CRLs in yeast, called SCF enzymes, employ a single E2 enzyme, Cdc34, to build poly-ubiquitin chains required for degradation. In contrast, six different huma

Externí odkaz: https://doaj.org/article/98a68f538710454382335ba50adf32c3

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Akademický článek

A feed forward loop enforces YAP/TAZ signaling during tumorigenesis

Autor: Mandeep K. Gill, Tania Christova, Ying Y. Zhang, Alex Gregorieff, Liang Zhang, Masahiro Narimatsu, Siyuan Song, Shawn Xiong, Amber L. Couzens, Jiefei Tong, Jonathan R. Krieger, Michael F. Moran, Alexandre R. Zlotta, Theodorus H. van der Kwast, Anne-Claude Gingras, Frank Sicheri, Jeffrey L. Wrana, Liliana Attisano

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)

The Hippo pathway is frequently dysregulated in cancer. Here, the authors identify NUAK2 as negative regulator of the Hippo pathway from a siRNA kinome screen and show that NUAK2 promotes YAP/TAZ nuclear localisation while NUAK2 is a transcriptional

Externí odkaz: https://doaj.org/article/d30df4cc14bf4f8f98f52cdb55527dcc

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Akademický článek

Real-time tracking of complex ubiquitination cascades using a fluorescent confocal on-bead assay

Autor: Joanna Koszela, Nhan T. Pham, David Evans, Stefan Mann, Irene Perez-Pi, Steven Shave, Derek F. J. Ceccarelli, Frank Sicheri, Mike Tyers, Manfred Auer

Publikováno v: BMC Biology, Vol 16, Iss 1, Pp 1-13 (2018)

Abstract Background The ubiquitin-proteasome system (UPS) controls the stability, localization and/or activity of the proteome. However, the identification and characterization of complex individual ubiquitination cascades and their modulators remain

Externí odkaz: https://doaj.org/article/6d2abde70b724d159ade739129cf8a40

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Akademický článek

An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase

Autor: Veronika Csizmok, Stephen Orlicky, Jing Cheng, Jianhui Song, Alaji Bah, Neda Delgoshaie, Hong Lin, Tanja Mittag, Frank Sicheri, Hue Sun Chan, Mike Tyers, Julie D. Forman-Kay

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)

The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereb

Externí odkaz: https://doaj.org/article/3ceb544c2e084e38929cafb11be01401

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