The cilium both releases and binds to extracellular vesicles (EVs) (Hogan et al., 2009; Pampliega et al., 2013; Wood et al., 2013; Wang et al., 2014). EVs may be used by cells as a form of intercellular communication and mediate a broad range of physiological and pathological processes (Gyorgy et al., 2011). The mammalian polycystins (PCs) localize to cilia as well as urinary EVs released from renal epithelial cells (Hogan et al., 2009). PC ciliary trafficking defects may be an underlying cause of autosomal dominant polycystic kidney disease (Cai et al., 2014), and ciliary-EV interactions have been proposed to play a central role in the biology of PKD (Chacon-Heszele et al., 2014). In C. elegans and mammals, PC1 and PC2 act in the same genetic pathway, act in a sensory capacity, localize to cilia, and are contained in secreted EVs, suggesting ancient conservation (Hogan et al., 2009; O'Hagan et al., 2014; Wang et al., 2014). However, the relationship between cilia and EVs and the mechanisms generating PC-containing EVs remain an enigma. In a forward genetic screen for regulators of C. elegans PKD-2 ciliary localization (Bae et al., 2008), we identified CIL-7, a myristoylated protein that regulates EV biogenesis. Loss of CIL-7 results in male mating behavioral defects, excessive accumulation of EVs in the lumen of the cephalic sensory organ, and failure to release PKD-2::GFP-containing EVs to the environment. Fatty acylation, such as myristoylation and palmitoylation, targets proteins to cilia and flagella (Godsel and Engman, 1999; Ramulu and Nathans, 2001; Tao et al., 2009; Tull et al., 2010; Maric et al., 2011; Wright et al., 2011; Cevik et al., 2013). The CIL-7 myristoylation motif is essential for CIL-7 function and for targeting CIL-7 to EVs. C. elegans is a powerful model to study ciliary EV biogenesis in vivo and to identify cis-targeting motifs such as myristoylation that are necessary for EV-cargo association and function.