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ZFIN ID: ZDB-PUB-120106-13
αE-catenin regulates cell-cell adhesion and membrane blebbing during zebrafish epiboly
Schepis, A., Sepich, D., and Nelson, W.J.
Date: 2012
Source: Development (Cambridge, England)   139(3): 537-46 (Journal)
Registered Authors: Sepich, Diane
Keywords: blebbing, cell-cell adhesion, cell migration, epiboly, gastrulation, zebrafish
MeSH Terms:
  • Animals
  • Cadherins/metabolism
  • Cell Adhesion
  • Cell Membrane/metabolism*
  • Cell Movement*
  • DNA-Binding Proteins/metabolism
  • Morphogenesis
  • Signal Transduction
  • Transcription Factors/metabolism
  • Zebrafish/growth & development*
  • Zebrafish/metabolism
  • Zebrafish Proteins/metabolism*
  • alpha Catenin/metabolism*
PubMed: 22190637 Full text @ Development
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ABSTRACT

αE-catenin is an actin-binding protein associated with the E-cadherin-based adherens junction that regulates cell-cell adhesion. Recent studies identified additional E-cadherin-independent roles of αE-catenin in regulating plasma membrane dynamics and cell migration. However, little is known about the roles of αE-catenin in these different cellular processes in vivo during early vertebrate development. Here, we examined the functions of αE-catenin in cell-cell adhesion, cell migration and plasma membrane dynamics during morphogenetic processes that drive epiboly in early Danio rerio (zebrafish) development. We show that depletion of αE-catenin caused a defect in radial intercalation that was associated with decreased cell-cell adhesion, in a similar manner to E-cadherin depletion. Depletion of αE-catenin also caused deep cells to have protracted plasma membrane blebbing, and a defect in plasma membrane recruitment of ERM proteins that are involved in controlling membrane-to-cortex attachment and membrane blebbing. Significantly, depletion of both E-cadherin and αE-catenin suppressed plasma membrane blebbing. We suggest that during radial intercalation the activities of E-cadherin and αE-catenin in the maintenance of membrane-to-cortex attachment are balanced, resulting in stabilization of cell-cell adhesion and suppression of membrane blebbing, thereby enabling proper radial intercalation.

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