Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-25134
Nature January 17, 1991; 349 (6306): 251-4.

In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase.

Gotoh Y , Nishida E , Matsuda S , Shiina N , Kosako H , Shiokawa K , Akiyama T , Ohta K , Sakai H .


Abstract
The protein kinase MAP kinase, also called MAP2 kinase, is a serine/threonine kinase whose activation and phosphorylation are induced by a variety of mitogens, and which is thought to have a critical role in a network of protein kinases in mitogenic signal transduction. A burst in kinase activation and protein phosphorylation may also be important in triggering the dramatic reorganization of the cell during the transition from interphase to mitosis. The interphase-metaphase transition of microtubule arrays is under the control of p34cdc2 kinase, a central control element in the G2-M transition of the cell cycle. Here we show that a Xenopus kinase, closely related to the mitogen-activated mammalian MAP kinase, is phosphorylated and activated during M phase of meiotic and mitotic cell cycles, and that the interphase-metaphase transition of microtubule arrays can be induced by the addition of purified Xenopus M phase-activated MAP kinase or mammalian mitogen-activated MAP kinase to interphase extracts in vitro.

PubMed ID: 1702878
Article link: Nature


Species referenced: Xenopus laevis
Genes referenced: cdk1 map2 mapk1