Disease relevance of Olfr73

• Analysis of cellular localization of known actin cross-linking proteins in mouse melanoma B16F1 cells revealed that fascin was specifically localized along the entire length of all filopodia, whereas other actin cross-linkers were not [1].

High impact information on Olfr73

• RNA interference of fascin reduced the number of filopodia, and remaining filopodia had abnormal morphology with wavy and loosely bundled actin organization [1].
• Fluorescence recovery after photobleaching of GFP-tagged wild-type and S39A fascin showed that dephosphorylated fascin underwent rapid cycles of association to and dissociation from actin filaments in filopodia, with t(1/2) < 10 s [1].
• Disruption of the N-terminal glycosylation site of the mOR-EG completely impaired its membrane trafficking to the cell surface [2].
• Each OR appears to recognize odorants based on similarities in molecular structures such that mOR-EG, a mouse OR, binds eugenol, vanillin, and some other structurally related odorants [2].
• Functional expression of the mOR-EG was greatly enhanced by addition of extra N-terminal glycosylation sequences [2].

Biological context of Olfr73

• These results show that fascin-1 is principally expressed in neural and mesenchymal derivatives during embryonic development [3].
• Fascin-1 is an actin-bundling protein that contributes to the architecture and function of cell protrusions and microfilaments in cell adhesion, interactions and motility [3].
• Localisation of fascin, the LIM and SH3 domain protein 1 (lasp-1), and lasp-2 to the bundles suggest their involvement in that organisation; however, their contributions remain unclear [4].
• The stimulatory effects of proteasome and autophagy inhibitors on mOREG function required export from the ER and trafficking through the biosynthetic pathway [5].
• This system, which utilizes signal transduction machinery coupled to OR activation in native olfactory sensory neurons, was used to demonstrate that degradation, both by the ubiquitin-proteasome system and autophagy, limits mOREG functional expression [5].

Anatomical context of Olfr73

• Fascin-1 has been studied in cultured cells and by biophysical methods, but little is known about its distribution and functions in vertebrate development [3].
• Fascin-1 was also present in the developing somites [3].
• At later stages, fascin-1 was expressed in different muscles of the face, skeletal muscles of the body, and in smooth muscle layers of several organs [3].
• These results indicated that fascin could be a reliable marker of paracortical dendritic cells in murine lymph nodes [6].
• Fibroblastic reticulum cells (FRCs), endothelial cells, histiocytic cells and lymphocytes in various stages of maturation were all fascin negative [6].

Associations of Olfr73 with chemical compounds

• Instead, an isoeugenol derivative produced during storage turned out to be a potent competitive antagonist of mOR-EG [7].

Other interactions of Olfr73

• Odorant responsiveness of a mouse olfactory receptor, mOR-EG, was investigated in various heterologous cells using a variety of detection methods [8].

References