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Reproduction, Fertility and Development Reproduction, Fertility and Development Society
Vertebrate reproductive science and technology
RESEARCH ARTICLE

The conformation and activation of Fyn kinase in the oocyte determine its localisation to the spindle poles and cleavage furrow

Mattan Levi A , Bernard Maro A B and Ruth Shalgi A C
+ Author Affiliations
- Author Affiliations

A Department of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Ramat-Aviv 69978, Tel-Aviv, Israel.

B Present address: CNRS, Paris, France.

C Corresponding author. Email: shalgir@post.tau.ac.il

Reproduction, Fertility and Development 23(7) 846-857 https://doi.org/10.1071/RD11033
Submitted: 7 February 2011  Accepted: 28 March 2011   Published: 19 August 2011

Abstract

Several lines of evidence imply the involvement of Fyn, a Src family kinase, in cell-cycle control and cytoskeleton organisation in somatic cells. By live cell confocal imaging of immunostained or cRNA-microinjected mouse oocytes at metaphase of the second meiotic division, membrane localisation of active and non-active Fyn was demonstrated. However, Fyn with a disrupted membrane-binding domain at its N-terminus was targeted to the cytoplasm and spindle in its non-active form and concentrated at the spindle poles when active. During metaphase exit, the amount of phosphorylated Fyn and of spindle-poles Fyn decreased and it started appearing at the membrane area of the cleavage furrow surrounding the spindle midzone, either asymmetrically during polar body II extrusion or symmetrically during mitosis. These results demonstrate that post-translational modifications of Fyn, probably palmitoylation, determine its localisation and function; localisation of de-palmitoylated active Fyn to the spindle poles is involved in spindle pole integrity during metaphase, whereas the localisation of N-terminus palmitoylated Fyn at the membrane near the cleavage furrow indicates its participation in furrow ingression during cytokinesis.

Additional keywords: meiosis, post-translational modifications.


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