Laminins in Epithelial Cell Polarization: Old Questions in Search of New Answers

Cold Spring Harb Perspect Biol. 2017 Oct 3;9(10):a027920. doi: 10.1101/cshperspect.a027920.

Abstract

Laminin, a basement membrane protein discovered in 1979, was shortly thereafter implicated in the polarization of epithelial cells in both mammals and a variety of lower organisms. To transduce a spatial cue to the intrinsic polarization machinery, laminin must polymerize into a dense network that forms the foundation of the basement membrane. Evidence suggests that activation of the small GTPase Rac1 by β1-integrins mobilizes laminin-binding integrins and dystroglycan to consolidate formation of the laminin network and initiate rearrangements of both the actin and microtubule cytoskeleton to help establish the apicobasal axis. A key coordinator of spatial signals from laminin is the serine-threonine kinase Par-1, which is known to affect dystroglycan availability, microtubule and actin organization, and lumen formation. The signaling protein integrin-linked kinase (ILK) may also play a role. Despite significant advances, knowledge of the mechanism by which assembled laminin produces a spatial signal remains fragmentary, and much more research into the complex functions of laminin in polarization and other cellular processes is needed.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Polarity*
  • Epithelial Cells / physiology*
  • Laminin / physiology*

Substances

  • Laminin