It is well established that guidance of axons during neuronal development is regulated by a variety of extracellular signals, goving cytoskeletal dynamics in growth cones. The actin and microtubule (MT) cytoskeleton have both been shown to play important roles. However, a growing body of work suggests that a critical issue is the proper coordination of changes within these two major cytoskeletal systems (reviewed in Cammara-ta et al., 2016). Previous studies led to the identification of a number of proteins involved in actin-microtubule crosstalk in neurons, in particular, several MT plus-end tracking proteins or+TIPs were shown to be at work. In addition to the well-known+TIP proteins, members of the formin protein family were also identified as regulators of actin and MT dynamics, initially in non-neuronal cells (reviewed in Bartolini and Gundersen, 2010) and more recently in neurons (Szikora et al., 2017). Most formins, belonging to the diaphanous related formin (DRF) subfamilies, share a conserved domain structure. They consist of the formin homology domains FH1 (required for profilin-ac-tin interaction) and FH2 (required for actin assembly and pro-tein dimerization), and a set of regulatory domains (GBD, DID, DD, DAD) (Figure 1A), which provide the means to control the spatial and temporal activity of the FH2 domain. Although formins were initially described as F-actin barbed end binding proteins, exhibiting an actin nucleation and elongation activity,subsequent work revealed that many formins have the potential to affect MT organization and/or dynamics in cellular systems, including neurons. Despite these advances, until recently, the contribution of formins to the govment of neuronal ac-tin-microtubule crosstalk remained largely elusive.