Phosphorylation by Cdk1 Increases the Binding of Eg5 to Microtubules In Vitro and in Xenopus Egg Extract Spindles

• DOI: 10.1371/journal.pone.0003936
• Publication Date: 2008-12-15T19:40:40Z
• Authors: Julie Cahu; Aurelien Olichon; Christian Hentrich; Henry Schek; Jovana Drinjakovic; Cunjie Zhang; Amanda Doherty-Kirby; Gilles Lajoie; Thomas Surrey
• Keywords: Kinesin; Spindle pole body

Background Motor proteins from the kinesin-5 subfamily play an essential role in spindle assembly during cell division of most organisms. These motors crosslink and slide microtubules spindle. Kinesin-5 are phosphorylated at a conserved site by Cyclin-dependent kinase 1 (Cdk1) mitosis. Xenopus laevis has also been reported to be Aurora A vitro. Methodology/Principal Findings We investigate here effect these phosphorylations on laevis, called Eg5. find that phosphorylation threonine 937 C-terminal tail Eg5 Cdk1 does not affect velocity Eg5, but strongly increases its binding assembled buffer. Likewise, this promotes egg extract spindles. This enhancement elevates amount spindles above critical level required for bipolar formation. furthermore serine 543 stalk is Conclusions/Significance results show direct interaction motor with microtubules. In extract, ensures enhanced targeting appears therefore be, least part, consequence upon Cdk1. findings advance our understanding regulation mitotic protein.