Mutation of the Cytoplasmic Domain of the Integrin β3 Subunit: DIFFERENTIAL EFFECTS ON CELL SPREADING, RECRUITMENT TO ADHESION PLAQUES …
J Ylänne, J Huuskonen, TE O'Toole… - Journal of Biological …, 1995 - ASBMB
The cytoplasmic domain of the β subunit of the α IIb β 3 integrin is required for cell spreading
on fibrinogen. Here we report that deletion of six amino acids from the COOH terminus of the
β 3 (I 757 TYRGT) totally abolished cell spreading and formation of adhesion plaques,
whereas retaining Ile 757 partially preserved these functions. We further found that
substitution of Tyr 747 with Ala also abolished α IIb β 3-mediated cell spreading. The effects
of these and other mutations on additional functions of α IIb β 3 were also studied …
on fibrinogen. Here we report that deletion of six amino acids from the COOH terminus of the
β 3 (I 757 TYRGT) totally abolished cell spreading and formation of adhesion plaques,
whereas retaining Ile 757 partially preserved these functions. We further found that
substitution of Tyr 747 with Ala also abolished α IIb β 3-mediated cell spreading. The effects
of these and other mutations on additional functions of α IIb β 3 were also studied …
