Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2132700 | Experimental Cell Research | 2006 | 9 Pages |
Abstract
Rhophilin-2 or p76RBE, 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.
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Authors
Séverine Steuve, Thalie Devosse, Elsa Lauwers, Jean-Marie Vanderwinden, Bruno André, Pierre J. Courtoy, Isabelle Pirson,