CD9-alpha6beta1 interactions in migratory parietal endoderm cells

Tetraspanins modulate the function of a variety of membrane proteins, including integrin receptors. We show here that the tetraspanin CD9 preferentially coimmunoprecipitates with the alpha6beta1 integrin heterodimer in F9-derived parietal endoderm cells in comparison to F9 stem cells. We also show t...

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Bibliographic Details
Published in:Cell communication & adhesion 2002-09, Vol.9 (5-6), p.249-258
Main Authors: Mulrooney, James P, Allen, Jessica, Bickelhaupt, Eric, Grabel, Laura B
Format: Article
Language:English
Subjects:
Animals
Antibodies - pharmacology
Antigens, CD - metabolism
Cell Membrane - metabolism
Cell Movement - physiology
Dimerization
Endoderm - cytology
Endoderm - metabolism
Focal Adhesions - metabolism
Integrin alpha6beta1 - metabolism
Macromolecular Substances
Membrane Glycoproteins - antagonists & inhibitors
Membrane Glycoproteins - metabolism
Mice
Neoplastic Stem Cells
Stem Cells - cytology
Stem Cells - metabolism
Tetraspanin-29
Vinculin - metabolism
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Summary:Tetraspanins modulate the function of a variety of membrane proteins, including integrin receptors. We show here that the tetraspanin CD9 preferentially coimmunoprecipitates with the alpha6beta1 integrin heterodimer in F9-derived parietal endoderm cells in comparison to F9 stem cells. We also show that CD9 function-blocking antibody inhibits parietal endoderm migration in an embryoid body outgrowth assay. In addition, both CD9 and alpha6beta1 colocalize with vinculin to apparent focal adhesion sites in parietal endoderm cells. The data presented here suggests a role for CD9 in localizing the integrin to the focal adhesion. In addition, the data suggest a role for CD9 in alpha6beta1 mediated migration of parietal endoderm.
ISSN:1541-9061