Rab11a is a small GTPase of the Ras superfamily involved in constitutive recycling pathways. Rab11a is involved in the regulation of several cellular processes, such as cytokinesis, phagocytosis, cell migration and ciliogenesis. However, its role in the secretory pathway of neuroendocrine cells has not been fully understood. We have previously reported that Rab11a coordinates the distribution of secretory vesicles (SV) at the plasma membrane in chromaffin cells, a well-known cellular system for neurosecretion. To study this further, we cotransfected chromaffin cells with Rab11a mutants with impaired GTP/GDP cycle together with fluorescently-tagged neuropeptide Y (NPY), as a marker of SV. By confocal microscopy, we observed a reduction in the amount of peripheral NPY in cells expressing S25N, a Rab11a dominant-negative mutant that cannot exchange GDP with GTP. To evaluate if SV trafficking dynamics were affected by Rab11a, we tracked GFP-tagged NPY in living chromaffin cells. We observed that SV mobility was reduced in cells expressing S25N, evidencing a role for Rab11a in the vesicle transport towards the plasma membrane. We propose that Rab11a plays a fundamental role in neurosecretion by modulating the availability of secretory vesicles at the plasma membrane through the coordination of the vesicular trafficking in chromaffin cells.