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The physiological function of epithelia depends on an asymmetric distribution of their membrane domains. Polarity proteins play a crucial role for distribution processes, however, little is known about their mobility in epithelial cells. In this study, we analyzed the intracellular and plasma-membrane-associated mobility of fluorescence-labeled Crb3A and Crb3B. Both variants belong to the Crumbs protein family, which control size and identity of apical membranes in epithelial cells. Fluorescence recovery after photo-bleaching measurements revealed different mobilities for the two Crb3 variants. They also differentially affected mobility and localization of the Pals1/Mpp5 protein, which binds to Crb3A but not to Crb3B. In addition, tracking of intracellular vesicles indicated that Crb3A containing vesicles are slightly more immobile than Crb3B ones. Taken together, our data revealed different intracellular mobility patterns for Crb3A and Crb3B. Copyright © 2016 Elsevier B.V. All rights reserved.


Ivona Djuric, Jan Peter Siebrasse, Ulf Schulze, Daniel Granado, Marc A Schlüter, Ulrich Kubitscheck, Hermann Pavenstädt, Thomas Weide. The C-terminal domain controls the mobility of Crumbs 3 isoforms. Biochimica et biophysica acta. 2016 Jun;1863(6 Pt A):1208-17

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PMID: 26975581

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