Differential recognition of secretory vesicles by annexins

Autor: F. Bartels, I. Waschulewski, J. M. Edwardson, Bastien D. Gomperts, C. Magnus, L. Nevalainen, R. Buccione, J. Pinxteren, L. Fletcher, I. Hide, C. E. Creutz, L. von Rueden, Giampietro Schiavo, Stephen J. Moss
Rok vydání: 1992
Předmět:
Zdroj: Biochemical and biophysical research communications
ISSN: 0006-291X
DOI: 10.1016/0006-291x(92)91199-z
Popis: The interactions of synexin, calpactin, and p68 (annexins VII, II, and VI) with zymogen granules and adrenal medullary chromaffin granules were compared. Synexin promoted the aggregation and fusion of both types of organelles. Calpactin inhibited the action of synexin on zymogen granules but would aggregate only chromaffin granules. p68 inhibited aggregation of chromaffin granules by calpactin and fusion of zymogen granules by synexin. The results demonstrate that these annexins, all of which bind acidic phospholipids, interact differently with different biological membranes and therefore may play specific and non-overlapping roles in cells where they are coexpressed.
Databáze: OpenAIRE