Suzan van Gerwen
Max Planck Society
7 Papers
Suzan van Gerwen is an academic researcher from Max Planck Society. The author has contributed to research in topics: Kinetochore & Spindle apparatus. The author has an hindex of 5, co-authored 7 publications.
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Papers
Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling
Ivana Primorac,John R. Weir,Elena Chiroli,Fridolin Gross,Ingrid Hoffmann,Suzan van Gerwen,Andrea Ciliberto,Andrea Musacchio +7 more
TL;DR: Bub3, a 7-bladed β-propeller, is the MELTP reader, providing the first detailed mechanistic insight into how phosphorylation promotes recruitment of checkpoint proteins to kinetochores.
Basis of catalytic assembly of the mitotic checkpoint complex
Alex C. Faesen,Maria Thanasoula,Stefano Maffini,Claudia Breit,Franziska Müller,Suzan van Gerwen,Tanja Bange,Andrea Musacchio +7 more
TL;DR: A near-complete SAC signalling system with purified components and monitored assembly of the MCC in real time is reconstituted and catalytic activation of the SAC depends on regulated protein–protein interactions that accelerate the spontaneous but rate-limiting conversion of MAD2 required for MCC assembly.
The pseudo GTPase CENP-M drives human kinetochore assembly
Federica Basilico,Stefano Maffini,John R. Weir,Daniel Prumbaum,Ana M. Rojas,Tomasz Zimniak,Anna De Antoni,Sadasivam Jeganathan,Beate Voss,Suzan van Gerwen,Veronica Krenn,Lucia Massimiliano,Alfonso Valencia,Ingrid R. Vetter,Franz Herzog,Stefan Raunser,Sebastiano Pasqualato,Andrea Musacchio +17 more
TL;DR: It is reported that a protein at the kinetochore–centromere interface, CENP-M, is structurally and evolutionarily related to small GTPases but is incapable of GTP-binding and conformational switching.
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KI motifs of human Knl1 enhance assembly of comprehensive spindle checkpoint complexes around MELT repeats.
TL;DR: The results show that KI motifs are enhancers of M ELT function in assembling SAC signaling complexes, and that they might have evolved to limit the expansion of MELT motifs by providing a more robust mechanism of Sac signaling around a single MELt.
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