O GPCR-mediated tastant detection, in OSNs disruption of the cAMP pathway leads to anosmia (Brunet et al., 1996; Belluscio et al., 1998; Wong et al., 2000). In olfactory cilia G13 co-localizes and is thought to interact with G1 and Golf (Kerr et al., 2008). Despite the fact that, the recombinant G113 dimer seems to be the second most potent activator of PLC- isoforms following G17 (Poon et al., 2009), the absence of a convincing demonstration of PLC- expression in OSNs suggests that in these cells G13 could play a further role. Kerr et al. reported that G13 interacts with Ric-8B, a guanine nucleotide exchange aspect for Golf, and hypothesized that by retaining Ric-8B in proximity of Golf-GTP, G13 would facilitate re-association of Ric-8B and Golf-GDP which ultimately would maximize the efficiency of that pathway. Our immunostaining experiments recommend that G13 interacts with ZO-1 temporarily for the duration of the maturation with the OSN. The effect this interaction could have on sensory signaling or OSN maturation remains to become investigated. Functional maturation is identified to take place in OSNs (Lee et al., 2011). This maturation could be correlated with signaling protein Cedryl acetate web trafficking and involve ZO-1 because it was previously implicated in maturation and regeneration in other cell sorts (Castillon et al., 2002; Kim et al., 2009). Beneath this situation it can be conceivable that the interaction amongst ZO-1 and G13 during OSN maturation could induce some functional modifications. In this case a tissue-specific G13 KO mouse model are going to be a worthwhile tool to help unravel the part of this protein in OSN function in vivo. Ultimately, in mouse cone and rod bipolar cells G13 seems to be distributed all through the cells when Go is concentrated in dendrites. The co-expression of G13 with G3, G4, and Go in ON cone bipolar cells which don’t include PLC- suggests that it might be involved in yet one more signaling pathway in these cells (Huang et al., 2003). In this tissue where ZO-1 expression has been reported as well (Ciolofan et al., 2006), it could be exciting to investigate whether these proteins are partly co-localized.CONCLUSIONIn the present study, we report the identification of 3 novel binding partners for G13. Moreover, we present the first proof in the expression of two of these proteins (GOPC and MPDZ) in taste bud cells. We anticipate that future function addressing the sequence of these interactions with G13 and their temporality will aid shed far more light around the precise part these proteins play in efficiently targeting G13 to selective subcellular places. By comparing the subcellular place of a number of these proteins in OSNs and neuroepithelial taste cells, our study points out attainable discrepancies in the mechanisms guiding protein trafficFrontiers in Cellular Neurosciencewww.frontiersin.orgJune 2012 | Volume 6 | Article 26 |Liu et al.ZO-1 interacts with Gand subcellular localization in these two cell kinds. These variations could not be Nemadectin custom synthesis surprising offered the differences in the origin (neuronal vs. epithelial) and the architecture of neuroepithelial taste cells and OSNs. In particular, we believe that the differential place of MPDZ and G13 in OSNs and TRCs reflects unique mechanisms at play in each varieties of sensory cells and delivers some clues as to what their function in these cells could be (transport vs. signalosome). Interestingly, MPDZ is believed to act as a scaffolding protein in the spermatozoa, a polarized cell capable of chemotaxis through taste and odora.
