Integrin Phosphorylation Is Modulated during the Differentiation of F-9 Teratocarcinoma Stem Cells

• Published in: The Journal of cell biology Vol. 108; no. 1; pp. 183 - 190
• Main Authors: Dahl, Stephen C., Grabel, Laura B.
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01.01.1989; The Rockefeller University Press
• Subjects: Actins; Actins - analysis; Animals; Biological and medical sciences; Cell culture techniques; Cell Differentiation; Cell differentiation, maturation, development, hematopoiesis; Cell physiology; Cells; Cellular differentiation; Cellular immunity; Cultured cells; Cytoskeleton - ultrastructure; Embryonal Carcinoma Stem Cells; Embryonic stem cells; fibronectin; Fibronectins - analysis; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Immunoblotting; integrin; Integrins; Molecular and cellular biology; Neoplastic Stem Cells - cytology; Neoplastic Stem Cells - drug effects; Neoplastic Stem Cells - metabolism; Phosphorylation; Precipitin Tests; Receptors, Fibronectin; Receptors, Immunologic - analysis; Receptors, Immunologic - metabolism; retinoic acid; Stem cells; Tretinoin - pharmacology; Tumor Cells, Cultured; Cell culture; Phosphorylation; Radiolabelling; Actins; Contractile protein; Glycoproteins; Cell differentiation; Malignant teratoma; Fibronectin; Proteins; Aminoacid; Immunoblotting assay; Cytoskeleton; Immunofluorescence; Localization
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.108.1.183

The retinoic acid-induced differentiation of F-9 teratocarcinoma cells in monolayer culture is accompanied by the accumulation of fibrillar fibronectin deposits, the appearance of a highly structured actin cytoskeleton, and the redistribution of integrin to apparent sites of substrate contact. We have studied the 140-kD fibronectin receptor during this process and report that although the integrin molecule is present in equivalent amounts before and after differentiation, the level of integrin phosphorylation decreases dramatically as the cells differentiate. This loss of phosphorylation coincides temporally with the observed changes in actin, fibronectin, and integrin organization. The phosphorylation state of integrin thus may mediate developmentally regulated cell-matrix interactions.