Abstract |
Although the involvement of alpha 6 beta 4, an integrin laminin receptor, in hemidesmosome organization has dominated the study of this integrin, recent studies are revealing novel functions for alpha 6 beta 4 in the migration of epithelial and carcinoma cells. The engagement of laminin by alpha 6 beta 4 can stabilize actin-rich protrusions and mediate traction forces necessary for cell movement. This integrin also has a significant impact on signaling molecules that stimulate migration and invasion, especially PI3-K and Rho GTPases. Activation of PI3-K by alpha 6 beta 4 enhances the formation of actin protrusions, and it may stimulate the function of other integrins, such as alpha 3 beta 1, that are also important for epithelial migration. Signaling through alpha 6 beta 4 may not always depend on the adhesive functions of this integrin, a possibility that has profound implications for migration and invasion because it implies that the ability of alpha 6 beta 4 to stimulate these processes is not limited to specific matrix environments.
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Authors | A M Mercurio, I Rabinovitz, L M Shaw |
Journal | Current opinion in cell biology
(Curr Opin Cell Biol)
Vol. 13
Issue 5
Pg. 541-5
(Oct 2001)
ISSN: 0955-0674 [Print] England |
PMID | 11544021
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S., Review)
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Chemical References |
- Antigens, Surface
- Integrin alpha6beta4
- Integrins
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Topics |
- Animals
- Antigens, Surface
(chemistry, physiology)
- Carcinoma
(pathology)
- Cell Adhesion
- Cell Movement
- Epithelial Cells
(physiology)
- Hemidesmosomes
(metabolism)
- Integrin alpha6beta4
- Integrins
(chemistry, physiology)
- Models, Biological
- Neoplasm Invasiveness
- Protein Structure, Tertiary
- Signal Transduction
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