scholarly journals Greatwall kinase at a glance

2018 ◽  
Vol 131 (20) ◽  
pp. jcs222364 ◽  
Author(s):  
Anna Castro ◽  
Thierry Lorca
Keyword(s):  
2013 ◽  
Vol 89 (3) ◽  
Author(s):  
Ying-Hua Li ◽  
Hyoeun Kang ◽  
Yong-Nan Xu ◽  
Young-Tae Heo ◽  
Xiang-Shun Cui ◽  
...  

PLoS Genetics ◽  
2016 ◽  
Vol 12 (9) ◽  
pp. e1006310 ◽  
Author(s):  
M. Kasim Diril ◽  
Xavier Bisteau ◽  
Mayumi Kitagawa ◽  
Matias J. Caldez ◽  
Sheena Wee ◽  
...  

Oncogene ◽  
2012 ◽  
Vol 32 (5) ◽  
pp. 537-543 ◽  
Author(s):  
T Lorca ◽  
A Castro
Keyword(s):  

2020 ◽  
Vol 39 (11) ◽  
Author(s):  
Nadia Hégarat ◽  
Adrijana Crncec ◽  
Maria F Suarez Peredo Rodriguez ◽  
Fabio Echegaray Iturra ◽  
Yan Gu ◽  
...  

2020 ◽  
Author(s):  
Mehmet Erguven ◽  
M. Kasim Diril

ABSTRACTMastl (Greatwall) kinase is an essential mitotic protein kinase. Mastl is an atypical member of AGC family with a unique long stretch of non-conserved middle region. The mechanism of its phosphorylation dependent activation has been studied in Xenopus egg extracts, revealing several phosphosites that were suggested to be crucial for kinase activation. These residues correspond to T193 and T206 in the activation loop, and S861 in the C-tail of mouse Mastl. By combining a chemically inducible knockout system to deplete the endogenous Mastl and a viral expression system to ectopically express the mutant variants, we obtained a viable knockout clone that expresses the S861A and S861D mutants. We observed that proliferation rates of the MastlS861A and MastlS861D clones were comparable. Our results have revealed that phosphorylation of the turn motif phosphosite (S861) is auxiliary and it is not indispensable for Mastl function.


2018 ◽  
Author(s):  
Nadia Hégarat ◽  
Adrijana Crncec ◽  
Maria F. Suarez Peredoa Rodri-guez ◽  
Fabio Echegaray Iturra ◽  
Yan Gu ◽  
...  

AbstractTwo mitotic Cyclins, A and B, exist in higher eukaryotes, but their specialised functions in mitosis are poorly understood. Using degron tags we analyse how acute depletion of these proteins affects mitosis. Loss of Cyclin A in G2-phase prevents the initial activation of Cdk1. Cells lacking Cyclin B can enter mitosis and phosphorylate most mitotic proteins, because of parallel PP2A:B55 phos-phatase inactivation by Greatwall kinase. The final barrier to mitotic establishment corresponds to nuclear envelope breakdown that requires a decisive shift in the balance of Cdk1 and PP2A:B55 activity. Beyond this point Cyclin B/Cdk1 is essential to phosphorylate a distinct subset mitotic Cdk1 substrates that are essential to complete cell division. Our results identify how Cyclin A, B and Greatwall coordinate mitotic progression by increasing levels of Cdk1-dependent substrate phos-phorylation.


2015 ◽  
Author(s):  
Rosa Della Monica ◽  
Roberta Visconti ◽  
Nando Cervone ◽  
Angela Flavia Serpico ◽  
Domenico Grieco

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