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Background Information: Fragile X mental retardation protein (FMRP) is a selective RNA binding protein that functions as a translational inhibitor. It also plays a role in directing the transport of a subset of mRNAs to their site of translation and several recent reports have implicated microtubule motor proteins in the transport of FMRP-messenger ribonucleoprotein (mRNP) granules in neurons. Earlier work reported the association of the actin-based motor protein myosin Va with FMRP granules., Results: Here, we follow up on this finding and confirm that myosin Va does in fact associate with FMRP and is required for its correct intracellular localisation. FMRP is concentrated in the perinuclear region of myosin Va-null mouse melanoma cells which contrasts starkly with the evenly distributed punctate pattern observed in wild-type cells. Similarly, overexpression of a dominant-negative mutant of myosin Va results in the accumulation of FMRP in large aggregate-like structures. FRAP experiments demonstrate that FMRP is largely immobile in the absence of myosin Va., Conclusions: Combining these data, we propose a model in which myosin Va and kinesin play key roles in the assembly and subsequent transport of FMRP granules along microtubules to the periphery of the cell. Myosin Va captures the complex onto peripheral actin structures and mediates the local delivery of the FMRP granule to the site of mRNA translation., (© 2013 Société Française des Microscopies and Société de Biologie Cellulaire de France. Published by John Wiley & Sons Ltd.)

Background Information: Rab GTPases are key coordinators of eukaryotic intracellular membrane trafficking. In their active states, Rabs localise to the cytoplasmic face of intracellular compartments where they regulate membrane trafficking processes. Many Rabs have been extensively characterised whereas others, such as Rab30, have to date received relatively little attention., Results: Here, we demonstrate that Rab30 is primarily associated with the secretory pathway, displaying predominant localisation to the Golgi apparatus. We find by time-lapse microscopy and fluorescence recovery after photobleaching studies that Rab30 is rapidly and continuously recruited to the Golgi. We also show that Rab30 function is required for the morphological integrity of the Golgi. Finally, we demonstrate that inactivation of Rab30 does not impair anterograde or retrograde transport through the Golgi., Conclusions: Taken together, these data illustrate that Rab30 primarily localises to the Golgi apparatus and is required for the structural integrity of this organelle., (Copyright © 2012 Soçiété Francaise des Microscopies and Société de Biologie Cellulaire de France.)

Background Information: Rab11 and Rab14 are two related Rab GTPases that are believed to function in endosomal recycling and Golgi/endosome transport processes. We, and others, have identified a group of proteins that interact with Rab11 and function as Rab11 effectors, known as the Rab11-FIPs (family interacting proteins). This protein family has been sub-classified into two groups - class I FIPs [FIP2, RCP (Rab coupling protein) and Rip11 (Rab11-interacting protein)] and class II FIPs (FIP3 and FIP4)., Results: In the present study we identify the class I FIPs as dual Rab-binding proteins by demonstrating that they also interact with Rab14 in a GTP-dependent manner. We show that these interactions are specific for the class I FIPs and that they occur via their C-terminal regions, which encompass the previously described RBD (Rab11-binding domain). Furthermore, we show that Rab14 significantly co-localizes with the TfnR (transferrin receptor) and that Rab14 Q70L co-localizes with Rab11a and with the class I FIPs on the ERC (endosomal recycling compartment) during interphase. Additionally, we show that during cytokinesis Rab14 localizes to the cleavage furrow/midbody., Conclusions: The data presented in the present study, which identifies the class I FIPs as the first putative effector proteins for the Rab14 GTPase, indicates greater complexity in the Rab-binding specificity of the class I FIP proteins.