par Steuve, Séverine 
;Devosse, Thalie ;Lauwers, Elsa ;Vanderwinden, Jean-Marie ;André, Bruno ;Courtoy, Pierre ;Pirson, Isabelle
Référence Experimental cell research, 312, 20, page (3981-3989)
Publication Publié, 2006-12
;Devosse, Thalie ;Lauwers, Elsa ;Vanderwinden, Jean-Marie ;André, Bruno ;Courtoy, Pierre ;Pirson, Isabelle Référence Experimental cell research, 312, 20, page (3981-3989)
Publication Publié, 2006-12
Article révisé par les pairs
| Résumé : | Rhophilin-2 or p76(RBE), a protein whose expression is induced by the cyclic AMP pathway in thyrocytes, contains several protein-protein interaction domains including HR-1, Bro1 and PDZ domains, and is a partner of RhoB in its GTP-bound form (Eur J Biochem, 269(24): 6241-9, 2002). We here define its subcellular localization and dissect the significance of its domains. By subcellular fractionation and colocalization experiments, rhophilin-2 is recruited to subcellular organelles by activated RhoB-GTP. As for its yeast homologue, Npi3/Bro1p, the Bro1 domain of rhophilin-2 is necessary to its recruitment to the vesicular structures, which are not labeled for EEA1 nor Lamp1, but well with the late endosome marker CD63. |
