Subcellular localization of Rap1 GTPase activator CalDAG-GEFI is orchestrated by interaction of its atypical C1 domain with membrane phosphoinositides

Autor: Aaron A. Cook, Ardeshir Goliaei, Lucia Stefanini, Marjorie Poggi, Brenda Temple, Florence Golesi, Wolfgang Bergmeier, Matthias Canault, Muzaddid Sarker, Sharon L. Campbell, Mohammad A. I. Khan

Publikováno v: J Thromb Haemost
Journal of Thrombosis and Haemostasis
Journal of Thrombosis and Haemostasis, 2019, 18 (3), pp.693-705. ⟨10.1111/jth.14687⟩
Journal of Thrombosis and Haemostasis, Wiley, 2019, 18 (3), pp.693-705. ⟨10.1111/jth.14687⟩

International audience; Background The small GTPase Rap1 and its guanine nucleotide exchange factor, CalDAG-GEFI (CDGI), are critical for platelet function and hemostatic plug formation. CDGI function is regulated by a calcium binding EF hand regulat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::173db87d767b36b08860af8d8757e2c1
https://pubmed.ncbi.nlm.nih.gov/31758832