title: The migratory behavior of avian embryonic cells does not require phosphorylation of the fibronectin-receptor complex.
abstract: When locomotory embryonic cells become stationary, they acquire new substratum-adhesion properties. In particular, the distribution of fibronectin receptors shifts from diffuse and highly mobile on the cell membrane to immobilized in close association with fibronectin molecules and cytoskeletal elements in focal contacts. Receptor phosphorylation has been proposed as a possible regulator of the interaction between the receptor and its intracellular and extracellular ligands. In the present study, we have compared the phosphorylation state of the fibronectin receptor in motile neural crest and somitic cells, in stationary somitic cells, and in Rous-sarcoma virus transformed-chick embryo fibroblasts, using immunoprecipitation following metabolic labeling. While no receptor phosphorylation was detected in motile embryonic cells, the beta subunit of the receptor was phosphorylated in stationary cells. This subunit was also highly phosphorylated in Rous-sarcoma virus-transformed chicken cells. These results suggest that phosphorylation of the fibronectin receptor cannot account for its distribution in the cell membrane and for the nature of the interactions between this receptor and its ligands in embryonic cells.
authors.affiliation: Centre National de la Recherche Scientifique, Ecole Normale Supérieure, Paris, France.
authors.forename: J L
authors.initials: JL
authors.lastname: Duband
authors.forename: S
authors.initials: S
authors.lastname: Dufour
authors.forename: K M
authors.initials: KM
authors.lastname: Yamada
authors.forename: J P
authors.initials: JP
authors.lastname: Thiery
mesh_terms: D000818:Animals; D002465:Cell Movement; D003370:Coturnix / Q000196:embryology*; D003598:Cytoskeletal Proteins / Q000378:metabolism; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D007163:Immunosorbent Techniques; D009432:Neural Crest / Q000166:cytology / Q000378:metabolism; D015688:Oncogene Protein pp60(v-src); D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011784:Quail / Q000196:embryology*; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic / Q000378:metabolism*; D012191:Retroviridae Proteins / Q000378:metabolism; D016608:Talin
chemical_list: D003598:Cytoskeletal Proteins; D005353:Fibronectins; D010710:Phosphates; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic; D012191:Retroviridae Proteins; D016608:Talin; D011505:Protein-Tyrosine Kinases; D015688:Oncogene Protein pp60(v-src)