IHEM   20887
INSTITUTO DE HISTOLOGIA Y EMBRIOLOGIA DE MENDOZA DR. MARIO H. BURGOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Rab11 is phosphorylated by classical and novel PKC isoenzymes upon sustained PMA stimulation
Autor/es:
PAVAROTTI M; CAPMANY A; COLOMBO, MI; DAMIANI MT
Lugar:
Chubut
Reunión:
Congreso; XLVI Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular; 2010
Institución organizadora:
SAIB
Resumen:
Bioinformatic analysis showed that Rab11 has high probability of
being phosphorylated by different PKC isoforms. In this work, we
present evidences that Rab11 is phosphorylated by cytosolic kinases
upon phorbol esters stimulation using an in vitro assay. Several
purified PKC isoforms directly phosphorylated Rab11 and the
results indicate that Rab11 was an adequate substrate for classical
PKCa and PKCbII but not PKCbI isoenzymes. In addition, the novel
PKCå and PKCç but not PKCä isoforms phosphorylated in vitro
Rab11 upon PMA activation, whereas the atypical PKCî isoenzyme
was unable to phosphorylate this GTPase. Rab11 was also
phosphorylated in vivo in PMA-treated HeLa cells. Interestingly,
overexpression of both Rab11 and the different PKC isoforms did
not alter transferrin recycling in unstimulated cells. However, a
sustained PMA-induced activation resulted in the translocation of
the classical PKCa and PKCbII to the endocytic recycling
compartment enriched in Rab11 and in the transferrin recycling
inhibition. This is the first report showing that Rab11 is
differentially phosphorylated by distinct PKC isoenzymes and, that
this post-translational modification could be a mechanism for the
regulation of intracellular trafficking pathways controlled by
Rab11.