Our previous study demonstrated that CaMKIIδ2 and Fyn physically interact via CaMKIIδ2's C ‐terminal “tail”. We also reported that this interaction between CaMKIIδ2 and Fyn positively mediates VSM cell motility. The purpose of this study is to better understand the mechanistic relationship between CaMKIIδ2 and Fyn and to clarify their cooperative role in migrating VSM cells. With immunofluorescence, we show that SiRNA depletion of CaMKIIδ in VSM cells attenuated PDGF‐dependent translocation of Fyn to peripheral membranes. Similarly, overexpression of CaMKIIδ6, which does not interact with Fyn, also reduced Fyn's ability to translocate to the plasma membrane in response to PDGF. Furthermore, overexpression of CaMKIIδ6 reduced VSM cell motility in both a scratch wound assay and a transwell assay. The rate of focal adhesion protein recruitment to focal adhesions is directly linked to cell motility. Using TIRF/FRAP in cells overexpressing GFP‐tagged Paxillin, we show that SiRNA mediated loss of CaMKIIδ2 or Fyn disrupted the kinetics of focal adhesion turnover. Stimulation of VSM cells with PDGF results in tyrosine phosphorylation of P130Cas and Paxillin, both known substrates of Fyn. Along with preventing Fyn translocation to the plasma membrane, overexpression of CaMKIIδ6 inhibited this PDGF‐dependent phosphorylation of P130Cas and Paxillin. Therefore, we conclude that CaMKIIδ2 “delivers” Fyn to peripheral membranes proximal to focal adhesions where Fyn modulates focal adhesion dynamics and subsequent VSM cell motility.