Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly

Autor: Elyse S. Fischer, Conny W. H. Yu, Johannes F. Hevler, Stephen H. McLaughlin, Sarah L. Maslen, Albert J. R. Heck, Stefan M. V. Freund, David Barford

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)

Formation of the mitotic checkpoint complex (MCC) is catalysed by a phosphorylation-dependent scaffold. This work provides structural details of how a tripartite Mad1:Bub1:Cdc20 complex presents Cdc20 to Mad2, triggering open-to-closed conversion of

Externí odkaz: https://doaj.org/article/25af90ef4aa84deab038bcc19c9bacc5

A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

Autor: Leo Kiss, Jingwei Zeng, Claire F. Dickson, Donna L. Mallery, Ji-Chun Yang, Stephen H. McLaughlin, Andreas Boland, David Neuhaus, Leo C. James

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)

The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme

Externí odkaz: https://doaj.org/article/470293ee22be4d32ba89b9430667e524

Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

Autor: Yi Liu, Gagan D. Gupta, Deepak D. Barnabas, Fikret G. Agircan, Shahid Mehmood, Di Wu, Etienne Coyaud, Christopher M. Johnson, Stephen H. McLaughlin, Antonina Andreeva, Stefan M. V. Freund, Carol V. Robinson, Sally W. T. Cheung, Brian Raught, Laurence Pelletier, Mark van Breugel

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)

Centriole duplication is tightly regulated in vivo, but the underlying molecular mechanisms are incompletely understood. Here the authors use high-resolution structural and imaging methods to show that CEP85 directly interacts with STIL and mediates

Externí odkaz: https://doaj.org/article/64d5bf6e3d9f4b17ae080b2ad6edfff9

The DNA-damage kinase ATR activates the FANCD2-FANCI clamp by priming it for ubiquitination

Autor: Tamara Sijacki, Pablo Alcón, Zhuo A. Chen, Stephen H. McLaughlin, Shabih Shakeel, Juri Rappsilber, Lori A. Passmore

Publikováno v: Nat Struct Mol Biol
Sijacki, T, Alcón, P, Chen, Z A, Mclaughlin, S H, Shakeel, S, Rappsilber, J & Passmore, L A 2022, ' The DNA-damage kinase ATR activates the FANCD2-FANCI clamp by priming it for ubiquitination ', Nature Structural & Molecular Biology, vol. 29, no. 9, pp. 881-890 . https://doi.org/10.1038/s41594-022-00820-9

DNA interstrand crosslinks are tumor-inducing lesions that block DNA replication and transcription. When crosslinks are detected at stalled replication forks, ATR kinase phosphorylates FANCI, which stimulates monoubiquitination of the FANCD2-FANCI cl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29732b28545880318807cd1c9a4253b6
https://doi.org/10.1038/s41594-022-00820-9

Cryo-EM structure of the complete inner kinetochore of the budding yeast point centromere

Autor: Tom Dendooven, Ziguo Zhang, Jing Yang, Stephen H. McLaughlin, Johannes Schwab, Sjors H.W. Scheres, Stanislau Yatskevich, David Barford

SummaryThe point centromere of budding yeast specifies assembly of the large multi-subunit kinetochore complex. By direct attachment to the mitotic spindle, kinetochores couple the forces of microtubule dynamics to power chromatid segregation at mito

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a34346ae6b6c35ac2b231d22ef1850f2
https://doi.org/10.1101/2022.12.12.520091