transduction and Dinaciclib intracellular signaling. These include: Inositol 1, 4, 5-trisphosphate receptor type 1; cell cycle progression protein 1; Rho guanine nucleotide exchange factor 17; and angiopoietinrelated protein 2. These interactions are of interest because Ric-3-mediated co-expression may promote subsequent signaling cascades. Inositol 1, 4, 5-trisphosphate receptor type 1 is associated with intracellular Ca2+ release and signaling. Nicotine stimulation of 7-nAChRs has been shown to lead to Ca2+ flux through IP3R type 1 and through activation of phospholipase C. In addition to the effect of 7-nAChRs on the activity of IP3Rs, it has also been shown that 7-nAChRs colocalize with IP3Rs in PC12 cells. IP3Rs have also been shown to colocalize with muscle-type nAChRs at the neuromuscular junction in rat skeletal muscle. Expanding on what was shown previously, the Eliglustat (hemitartrate) association of IP3Rs with 7-nAChR identified in this study reflects a direct interaction between the IP3R and the 7-nAChR interactome. Cell cycle progression protein 1, Rho guanine nucleotide exchange factor 17, and angiopoietin-related protein 2 are associated with RhoA GTPases and may be involved in a number of processes. Angiopoietin-related protein 2, for example, has been linked to cellular processes such as angiogenesis and cell motility, and members of the small RhoA GTPase family participate in the endocytosis of muscle-type nAChRs. Fourteen proteins were identified that are not currently linked to 7-nAChR surface expression, signal transduction/intracellular signaling, or protein catabolism and/or autophagy. These fourteen proteins are associated with the cytoskeletal organization; developmental processes; ion transport; nucleobase, nucleoside, nucleotide, and nucleic acid metabolic processes; biosynthetic processes; response to stress, or do not currently have a well-defined associated biological process. Several of the additional proteins identified are associated with the cytoskeleton and developmental processes and may be involved in the subcellular localization of nAChRs. Keratin however is often considered to be non-specific contaminant in mass spectrometry investigations and these proteins
