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Published 5 June 2006. doi:10.1083/jcb.200509019
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 5, 767-780
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Article

 Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of ß1-integrins

Teijo Pellinen1,2, Antti Arjonen1,2, Karoliina Vuoriluoto1,2, Katja Kallio1,2, Jack A.M. Fransen3, and Johanna Ivaska1,2

1 VTT Technical Research Centre of Finland, Medical Biotechnology, Turku FIN-20520, Finland
2 University of Turku Centre for Biotechnology, Turku FIN-20520, Finland
3 Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center St. Radboud, University of Nijmegen, Nijmegen, Netherlands

Correspondence to Johanna Ivaska: johanna.ivaska{at}vtt.fi

Dynamic turnover of integrin cell adhesion molecules to and from the cell surface is central to cell migration. We report for the first time an association between integrins and Rab proteins, which are small GTPases involved in the traffic of endocytotic vesicles. Rab21 (and Rab5) associate with the cytoplasmic domains of {alpha}-integrin chains, and their expression influences the endo/exocytic traffic of integrins. This function of Rab21 is dependent on its GTP/GDP cycle and proper membrane targeting. Knock down of Rab21 impairs integrin-mediated cell adhesion and motility, whereas its overexpression stimulates cell migration and cancer cell adhesion to collagen and human bone. Finally, overexpression of Rab21 fails to induce cell adhesion via an integrin point mutant deficient in Rab21 association. These data provide mechanistic insight into how integrins are targeted to intracellular compartments and how their traffic regulates cell adhesion.

Abbreviations used in this paper: MVB, multivesicular body; Rluc, Renilla luciferase; shRNA, short hairpin RNA; TIRFM, total internal reflection fluorescence microscopy; WT, wild type.


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