Rab11-FIP3 is a cell cycle-regulated phosphoprotein

Collins, L.L., Simon, G., Matheson, J., Wu, C., Miller, M.C., Otani, T., Yu, X., Hayashi, S., Prekeris, R. and Gould, G.W. (2012) Rab11-FIP3 is a cell cycle-regulated phosphoprotein. BMC Cell Biology, 13(1), p. 4. (doi: 10.1186/1471-2121-13-4) (PMID:22401586) (PMCID:PMC3310825)

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Publisher's URL: http://dx.doi.org/10.1186/1471-2121-13-4

Abstract

<b>BACKGROUND:</b> Rab11 and its effector molecule, Rab11-FIP3 (FIP3), associate with recycling endosomes and traffic into the furrow and midbody of cells during cytokinesis. FIP3 also controls recycling endosome distribution during interphase. Here, we examine whether phosphorylation of FIP3 is involved in these activities.<p></p> <b>RESULTS:</b> We identify four sites of phosphorylation of FIP3 in vivo, S-102, S-280, S-347 and S-450 and identify S-102 as a target for Cdk1-cyclin B in vitro. Of these, we show that S-102 is phosphorylated in metaphase and is dephosphorylated as cells enter telophase. Over-expression of FIP3-S102D increased the frequency of binucleate cells consistent with a role for this phospho-acceptor site in cytokinesis. Mutation of S-280, S-347 or S-450 or other previously identified phospho-acceptor sites (S-488, S-538, S-647 and S-648) was without effect on binucleate cell formation and did not modulate the distribution of FIP3 during the cell cycle. In an attempt to identify a functional role for FIP3 phosphorylation, we report that the change in FIP3 distribution from cytosolic to membrane-associated observed during progression from anaphase to telophase is accompanied by a concomitant dephosphorylation of FIP3. However, the phospho-acceptor sites identified here did not control this change in distribution.<p></p> <b>CONCLUSIONS:</b> Our data thus identify FIP3 as a cell cycle regulated phosphoprotein and suggest dephosphorylation of FIP3 accompanies its translocation from the cytosol to membranes during telophase. S102 is dephosphorylated during telophase; mutation of S102 exerts a modest effect on cytokinesis. Finally, we show that de/phosphorylation of the phospho-acceptor sites identified here (S-102, S-280, S-347 and S-450) is not required for the spatial control of recycling endosome distribution or function.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Gould, Professor Gwyn and Yu, Miss Xinzi and Matheson, Dr Johanne and Miller, Mrs Marie and Collins, Dr Louise
Authors: Collins, L.L., Simon, G., Matheson, J., Wu, C., Miller, M.C., Otani, T., Yu, X., Hayashi, S., Prekeris, R., and Gould, G.W.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:BMC Cell Biology
ISSN:1471-2121
ISSN (Online):1471-2121
Published Online:08 March 2012
Copyright Holders:Copyright © 2012 Collins et al.: licensee BioMed Central Ltd.
First Published:First published in BMC Cell Biology 13(1):4
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
403161The role of Rab 11-FIP3 and Rab 11-FIP4 in cytokinesisGwyn GouldBiotechnology and Biological Sciences Research Council (BBSRC)BB/D000017/1Institute of Molecular Cell and Systems Biology