Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility.
We have analyzed the interaction of neural crest cells with fragments of fibronectin corresponding to the different spliced variants of the COOH-terminal cell-binding domain (COOH-ter CBD). We have shown that this domain can support cell adhesion and migration and that both the IIICS and HepII regions are involved in these events. The rate of locomotion is high, although undirectional, compared to that of whole fibronectin. Interactions with the COOH-ter CBD are controlled by alpha4beta1 and maybe other beta1 integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.
Beauvais-Jouneau
A
A
Subcellular Structure and Cellular Dynamics, UMR 144, CNRS-Institut Curie, Paris, France.
Delouvée
A
A
Craig
S E
SE
Humphries
M J
MJ
Thiery
J P
JP
Dufour
S
S
D000818:Animals; D002448:Cell Adhesion / Q000235:genetics; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism*; D002465:Cell Movement / Q000235:genetics; D002478:Cells, Cultured; D005353:Fibronectins / Q000235:genetics / Q000378:metabolism*; D014644:Genetic Variation; D007150:Immunohistochemistry; D019012:Integrin beta1 / Q000302:isolation & purification; D009432:Neural Crest / Q000166:cytology / Q000502:physiology*; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D011784:Quail / Q000196:embryology
D015815:Cell Adhesion Molecules; D005353:Fibronectins; D019012:Integrin beta1; D010446:Peptide Fragments