Participation of membrane skeleton proteins in aggregation of epidermal growth factor receptors in A431 cells.
Polyclonal antibody against alpha-spectrin of chicken erythrocytes was prepared. This antibody as well as anti-vinculin and anti-annexin I and II, were used for localization of the antigens in A431 cells during translocation of epidermal growth factor receptors (EGF-Rs) on cell surface. During aggregation of EGF-Rs only spectrin and actin aggregates colocalized with the "capped" receptors in adherent as well as in suspended cells. Physiological implication of spectrin involvement in EGF-Rs redistribution in A431 cells is discussed.
Kwiatkowska
K
K
Nencki Institute of Experimental Biology, Department of Cell Biology, Warsaw, Poland.
Khrebtukova
I A
IA
Sobota
A
A
D000199:Actins / Q000502:physiology*; D000818:Animals; D000906:Antibodies / Q000032:analysis; D002478:Cells, Cultured; D002645:Chickens; D004817:Epidermis; D066246:ErbB Receptors / Q000502:physiology*; D004910:Erythrocyte Membrane; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology*; D011940:Receptor Aggregation / Q000502:physiology*; D013049:Spectrin / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology*
D000199:Actins; D000906:Antibodies; D008565:Membrane Proteins; D013049:Spectrin; D066246:ErbB Receptors