RAB14 is involved in the trafficking of GLUT4 to the plasma membrane and also contributes to cell migration by regulating the trafficking of ADAM10, a metalloendopetidase that cleaves a number of cell surface proteins including the adherens junction components N-cadherin (Reed et al, 2013; Brewer et al, 2016; Linford et al, 2012; Lu et al, 2012; Maretzky et al, 2005; Reiss et al, 2005; Gutwein et al, 2010; Rabquer et al, 2010). DENND6A and B, also known as FAM116A and B, show RAB14 GEF activity in vitro and are required for RAB14 localization and activity in vivo (Linford et al, 2012; reviewed in Ishida et al, 2016). Interaction of RAB14:GDP with its GEFs promotes release of GDP, allowing GTP to bind, and precludes the interaction of RAB14 with GDI and CHM proteins.

RUN and FYVE domain-containing protein 1 (RUFY1, aka RABIP4, ZFYVE12), together with Ras-related proteins RAB4A, 5 and 14, could play an important role in GLUT4 trafficking in adipocytes and skeletal muscle (Kitagishi & Matsuda 2013, Larance et al. 2005, Mari et al. 2006, Fouraux et al. 2004).

As inferred from mouse, GLUT4 (SLC2A4) initially translocates from endosomes to insulin-responsive vesicles (IRVs, GSVs). RAB11 appears to play a role in this process. IRVs bearing GLUT4 are then translocated across the cortical actin network to the plasma membrane. Unconventional myosin 5A (MYO5A) interacts with RAB10 or RAB8A on the vesicle and participates in transport of the IRV. Myosin 1C appears to act close to the plasma membrane and may facilitate fusion of the vesicle with the plasma membrane. RAB:GTP complexes coupled to the vesicles may interact with myosins to regulate their activity. Non-muscle myosin IIA (MYH9) appears to interact with the SNAP23 complex to dock the IRV at the inner membrane face.
As inferred from mouse (Zeigerer et al. 2002) and rat (Uhlig et al. 2005), RAB11A enhances translocation of GLUT4 to the plasma membrane by mobilizing GLUT4 (SLC2A4) from endosomes to insulin responsive vesicles.
As inferred from mouse (Sano et al. 2007) and rat (Ishikura et al. 2007, Ishikura and Klip 2008, Sun et al. 2010), RAB:GTP activates translocation of GLUT4 (SLC2A4) to the plasma membrane, possibly by interacting with myosins. RAB8A, RAB10, and RAB14 predominate in 3T3-L1 adipocytes; RAB13 predominates in L6 muscle cells.
As inferred from mouse, TC10 participates in the translocation and docking of GLUT4 (SLC2A4) vesicles at the plasma membrane (Chang et al. 2007).
As inferred from mouse (Ueda et al. 2008, Ueda et al. 2010) and rat (Chiu et al. 2010), RAC1:GTP enhances translocation of GLUT4 (SLC2A4) to the plasma membrane by causing actin remodeling that requires ARP2/3. The exact mechanism of RAC1 action is unknown.

In adipocytes and myocytes insulin signaling causes intracellular vesicles carrying the GLUT4 (SLC2A4) glucose transporter to translocate to the plasma membrane, allowing the cells to take up glucose from the bloodstream (reviewed in Zaid et al. 2008, Leney and Tavare 2009, Bogan and Kandror 2010, Foley et al. 2011, Hoffman and Elmendorf 2011, Kandror and Pilch 2011, Jaldin-Fincati et al. 2017). In myocytes muscle contraction alone can also cause translocation of GLUT4.
Though the entire pathway leading to GLUT4 translocation has not been elucidated, several steps are known. Insulin activates the kinases AKT1 and AKT2. Muscle contraction activates the kinase AMPK-alpha2 and possibly also AKT. AKT2 and, to a lesser extent, AKT1 phosphorylate the RAB GTPase activators TBC1D1 and TBC1D4, causing them to bind 14-3-3 proteins and lose GTPase activation activity. As a result RAB proteins (probably RAB8A, RAB10, RAB14 and possibly RAB13) accumulate GTP. The connection between RAB:GTP and vesicle translocation is unknown but may involve recruitment and activation of myosins.
Myosins 1C, 2A, 2B, 5A, 5B have all been shown to play a role in translocating GLUT4 vesicles near the periphery of the cell. Following docking at the plasma membrane the vesicles fuse with the plasma membrane in a process that depends on interaction between VAMP2 on the vesicle and SNAP23 and SYNTAXIN-4 at the plasma membrane.