The Rab proteins constitute a large family of small GTPase known to be involved in the regulation of several steps of intracellular membrane traffic. All Rabs localize at specific subcellular compartments and their distribution is crucial for the specificity and directionality of membrane traffic (i.e. secretion, endocytosis, recycling etc.). In particular, Rab14 is the mostrecently discovered member of the Rab11 subfamily that has been associated with different aspects of the endocytic recycling pathway. Rab14 localizes at the trans-Golgi network where it is involved in the membrane recycling between the Golgi complex and the endosomal compartment. Here we have identified Rab14 as a novel substrate of PARP12, a mono ADP-ribosyl transferase mainly localized at the Golgi complex. The physiological functions of PARP12 are not yet completely elucidated. With this study we demonstrate that PARP12 is able to interact and modify Rab14 and that its depletion impairs Rab14 modification. This process alters Rab14 localization, which in turn affects the membrane flow trough the recycling endosomes. Overall our data reveal that mono ADP-ribosylation is a new posttranslation modification of Rab14 and underline a role for PARP12 in the Rab14-mediated intracellular membrane traffic.
RAB14, A NOVEL SUBSTRATE OF THE mART PARP12
Annunziata Corteggio;Giovanna Grimaldi;Giuliana Catara;Daniela Corda
2016
Abstract
The Rab proteins constitute a large family of small GTPase known to be involved in the regulation of several steps of intracellular membrane traffic. All Rabs localize at specific subcellular compartments and their distribution is crucial for the specificity and directionality of membrane traffic (i.e. secretion, endocytosis, recycling etc.). In particular, Rab14 is the mostrecently discovered member of the Rab11 subfamily that has been associated with different aspects of the endocytic recycling pathway. Rab14 localizes at the trans-Golgi network where it is involved in the membrane recycling between the Golgi complex and the endosomal compartment. Here we have identified Rab14 as a novel substrate of PARP12, a mono ADP-ribosyl transferase mainly localized at the Golgi complex. The physiological functions of PARP12 are not yet completely elucidated. With this study we demonstrate that PARP12 is able to interact and modify Rab14 and that its depletion impairs Rab14 modification. This process alters Rab14 localization, which in turn affects the membrane flow trough the recycling endosomes. Overall our data reveal that mono ADP-ribosylation is a new posttranslation modification of Rab14 and underline a role for PARP12 in the Rab14-mediated intracellular membrane traffic.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
