Researcher
Morpho-functional organisation and regulation of the biosynthetic pathway Lab
Phone: +39 0816132713
Email:
rosaria.dimartino@cnr.it
r.dimartino@ieos.cnr.it
Protein trafficking is a finely tuned process that allows proteins to reach their subcellular destination with high spatiotemporal precision and appropriate post-translational modifications. The Golgi complex plays a fundamental role in the secretory pathway and acts as a “signaling organelle”. In this scenario, cargo proteins that are synthesized, modified and transported through the secretory pathway, act as signaling inputs thus activating specific signaling cascades to optimize their own transport process, giving rise to “autoregulatory circuits”. Our group has previously identified many of these circuits, and they are present at every important step in the secretion process, such as ER export and intra-Golgi transport. My research is focused on identifying and characterizing the signaling circuits that regulate specific steps of the secretory pathway: the processes of TGN export and sorting. This process requires specific molecular machinery depending on the class of proteins that need to be transported, such as apical or basolateral proteins. Indeed, we identified GPRC5A, an orphan GPCR localized in the TGN, as a key molecule for the correct release of basolateral proteins by regulating the recruitment and activation of the PKD signaling pathway. Our results suggest a role of GPRC5A as a “sensor” of basolateral proteins to promote its export from the TGN. It should be noted that dysregulation in the TGN sorting machinery has been associated with several human diseases, including cancer progression and neurodegeneration, so we are investigating the role of our regulatory circuit in both contexts.
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