Cortactin Is Necessary for E-Cadherin-Mediated Contact Formation and Actin Reorganization

Classical cadherin adhesion molecules are key determinants of cell-cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact...

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Bibliographic Details
Published in:The Journal of cell biology 2004-03, Vol.164 (6), p.899-910
Main Authors: Helwani, Falak M., Kovacs, Eva M., Paterson, Andrew D., Verma, Suzie, Ali, Radiya G., Fanning, Alan S., Weed, Scott A., Yap, Alpha S.
Format: Article
Language:English
Subjects:
Actins
Actins - metabolism
Adhesives
Animals
Binding Sites
Biochemistry
Cadherins
Cadherins - genetics
Cadherins - metabolism
Cell adhesion & migration
Cell Adhesion - physiology
Cell Line
Cell lines
Cell Membrane - metabolism
Cell Size
Cells
Cellular biology
Cellular immunity
Chickens
CHO cells
Cortactin
Cricetinae
Dogs
Epithelial cells
Fluorescence
Humans
Intercellular Junctions - chemistry
Intercellular Junctions - metabolism
Macromolecular Substances
Microfilament Proteins - genetics
Microfilament Proteins - metabolism
Protein Structure, Tertiary
Pseudopodia
RNA Interference
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Summary:Classical cadherin adhesion molecules are key determinants of cell-cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact zone extension entails active cooperation between cadherin adhesion and the force-generating capacity of the actin cytoskeleton. Cortactin has recently emerged as an important regulator of actin dynamics in several forms of cell motility. We now report that cortactin is recruited to cell-cell adhesive contacts in response to homophilic cadherin ligation. Notably, cortactin accumulates preferentially, with Arp2/3, at cell margins where adhesive contacts are being extended. Recruitment of cortactin is accompanied by a ligation-dependent biochemical interaction between cortactin and the cadherin adhesive complex. Inhibition of cortactin activity in cells blocked Arp2/3-dependent actin assembly at cadherin adhesive contacts, significantly reduced cadherin adhesive contact zone extension, and perturbed both cell morphology and junctional accumulation of cadherins in polarized epithelia. Together, our findings identify a necessary role for cortactin in the cadherin-actin cooperation that supports productive contact formation.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200309034