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Myosin Vb and Rab11a regulate phosphorylation of ezrin in enterocytes

Dhekne, H. S., Hsiao, N-H., Roelofs, P., Kumari, M., Slim, C. L., Rings, E. H. H. M. & van IJzendoorn, S. C. D., 1-Mar-2014, In : Journal of Cell Science. 127, 5, p. 1007-1017 11 p.

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Microvilli at the apical surface of enterocytes allow the efficient absorption of nutrients in the intestine. Ezrin activation by its phosphorylation at T567 is important for microvilli development, but how such ezrin phosphorylation is controlled is not well understood. We demonstrate that a subset of kinases that phosphorylate ezrin closely co-distributes with apical recycling endosome marker Rab11a in the subapical domain. Expression of dominant-negative Rab11a mutant or depletion of the Rab11a-binding motor protein myosin Vb prevents the subapical enrichment of Rab11a and these kinases and inhibits ezrin phosphorylation and microvilli development, without affecting the polarized distribution of ezrin itself. We observe a similar loss of the subapical enrichment of Rab11a and the kinases and reduced phosphorylation of ezrin in microvillus inclusion disease, which is associated with MYO5B mutations, intestinal microvilli atrophy and malabsorption. Thus, part of the machinery for ezrin activation depends on recycling endosomes controlled by myosin Vb and Rab11a which, we propose, might act as subapical signaling platforms that enterocytes use to regulate development of microvilli and maintain human intestinal function.
Original languageEnglish
Pages (from-to)1007-1017
Number of pages11
JournalJournal of Cell Science
Volume127
Issue number5
Publication statusPublished - 1-Mar-2014

    Keywords

  • Apical, Enterocyte, Microvilli, Microvillus inclusion disease, Recycling endosome, MICROVILLUS INCLUSION DISEASE, INTESTINAL EPITHELIAL-CELLS, RECYCLING ENDOSOMES, PLASMA-MEMBRANE, MYO5B MUTATIONS, ERM PROTEINS, POLARITY, ATROPHY, COMPLEX, POLARIZATION

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