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The Crumbs3 Complex

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Cell Polarity 1

Abstract

Epithelial layers have allowed the evolution of metazoans by promoting complex multicellularity and protection from the environment. This essential role for epithelia relies on their ability to build an apical surface facing the outside world and a basolateral surface connecting cells together to coordinate their movements and resistance to stress. These epithelial features are dependent on several protein complexes for their establishment and maintenance. Among these protein complexes, one complex contains an apical transmembrane protein, Crumbs, that plays an essential role for the proper organization of tight junctions, apical morphology, or cell and tissue growth. In this chapter we will review how Crumbs3, one of the Crumbs proteins, both recruits adapter proteins essential for the building of tight or adherens junctions in vertebrates and interacts with the subapical actin cytoskeleton. These functions are broadly conserved in animals from flies to human, and it remains a challenge to understand all the molecular mechanisms by which Crumbs3 and its partners participate in the building of a functional epithelial sheet to keep body homeostasis and to allow for morphogenetic events as essential as gastrulation.

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Abbreviations

aPKC:

Atypical protein kinase C

Crb:

Crumbs

FERM:

4.1-Ezrin-radixin-moesin

IMCD3:

Inner medullary collecting duct

KO:

Knockout

MAGUK:

Membrane-associated guanylate kinase

MDCK:

Madin-Darby canine kidney

MPP5:

Membrane-associated palmitoylated proteins

OLM:

Outer limiting membrane

PALS1:

Protein associated with Lin-7

PAR6:

Partition defective-6

PATJ:

PALS1-associated tight junction protein

PDZ:

PSD-95, discs large, zona occludens 1

RP12:

Retinitis pigmentosa group 12

Sdt:

Stardust

TJ:

Tight junction

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Acknowledgments

We thank the Le Bivic Lab members for the critical reading of the manuscript. ALB laboratory is supported by the CNRS (UMR7288) and Aix-Marseille University and is an “Equipe labellisée 2008 de la Ligue Nationale contre le Cancer.” This work has been carried out in the framework of the Labex INFORM (ANR-11-LABX-0054). B. Vacca is supported by Biotechnology and Biological Sciences Research Council (BBSRC).

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Correspondence to André Le Bivic .

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Vacca, B., Barthélémy-Requin, M., Burcklé, C., Massey-Harroche, D., Bivic, A.L. (2015). The Crumbs3 Complex. In: Ebnet, K. (eds) Cell Polarity 1. Springer, Cham. https://doi.org/10.1007/978-3-319-14463-4_3

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