Aurora A phosphorylates Ndel1 to reduce the levels of Mad1 and NuMA at spindle poles

Autor: Paweł Ł. Janczyk, Eliza Żyłkiewicz, Henry De Hoyos, Thomas West, Daniel R. Matson, Won-Chan Choi, Heather M. Raimer Young, Zygmunt S. Derewenda, P. Todd Stukenberg
Rok vydání: 2023
Předmět:
Zdroj: Molecular Biology of the Cell. 34
ISSN: 1939-4586
1059-1524
DOI: 10.1091/mbc.e21-09-0438
Popis: Dynein inactivates the spindle assembly checkpoint (SAC) by transporting checkpoint proteins away from kinetochores toward spindle poles in a process known as "stripping." We find that inhibition of Aurora A kinase, which is localized to spindle poles, enables the accumulation of the spindle checkpoint activator Mad1 at poles where it is normally absent. Aurora kinases phosphorylate the dynein activator NudE neurodevelopment protein 1 like 1 (Ndel1) on Ser285 and Mad1 accumulates at poles when Ndel1 is replaced by a nonphosphorylatable mutant in human cells. The pole focusing protein NuMA, transported to poles by dynein, also accumulates at poles in cells harboring a mutant Ndel1. Phosphorylation of Ndel1 on Ser285 is required for robust spindle checkpoint activity and regulates the poles of asters in
Databáze: OpenAIRE