Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/105810
Title: Phosphorylation of Rab5a protein by protein kinase Cϵ is crucial for T-cell migration
Authors: Ong, Seow Theng
Freeley, Michael
Skubis-Zegadło, Joanna
Fazil, Mobashar Hussain Urf Turabe
Kelleher, Dermot
Fresser, Friedrich
Baier, Gottfried
Verma, Navin Kumar
Long, Aideen
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2014
Source: Ong, S. T., Freeley, M., Skubis-Zegadło, J., Fazil, M. H. U. T., Kelleher, D., Fresser, F., et al. (2014). Phosphorylation of Rab5a protein by protein kinase Cϵ is crucial for T-cell migration. Journal of biological chemistry, 289(28), 19420-19434.
Series/Report no.: Journal of biological chemistry
Abstract: Rab GTPases control membrane traffic and receptor-mediated endocytosis. Within this context, Rab5a plays an important role in the spatial regulation of intracellular transport and signal transduction processes. Here, we report a previously uncharacterized role for Rab5a in the regulation of T-cell motility. We show that Rab5a physically associates with protein kinase C ε (PKC ε ) in migrating T-cells. Following stimulation of T- cells through the integrin LFA-1 or the chemokine receptor CXCR4, Rab5a is phosphorylated on a N-terminal T7 site by PKC ε . Both Rab5a and PKC ε dynamically interact at the centrosomal region of migrating cells, and PKC ε -mediated phosphorylation on T7 regulates Rab5a trafficking to the cell leading edge. Further, we demonstrate that Rab5a T7 phosphorylation is functionally necessary for Rac1 activation, actin rearrangement and T- cell motility. We present a novel mechanism by which a PKC ε -Rab5a-Rac1 axis regulates cytoskeleton remodelling and T-cell migration, both of which are central for the adaptive immune response.
URI: https://hdl.handle.net/10356/105810
http://hdl.handle.net/10220/20966
DOI: 10.1074/jbc.M113.545863
Rights: © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Biological Chemistry, The American Society for Biochemistry and Molecular Biology, Inc. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1074/jbc.M113.545863].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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