Protein Extraction and Western Blotting

For protein extraction, tissues were homogenized in ice-cold RIPA buffer. Total protein was quantified using the DC Protein Assay according to the manufacturer’s instructions (BioRad, Hercules, CA). Western blotting was performed as previously described with minor modifications^{13 (link)}. Briefly, 10 % Bis-Tris polyacrylamide gels (NuPage, Invitrogen) were equiloaded with 10–30μg of protein, electrophoresed at 200V, and electrotransferred to PVDF membranes. After blocking with 5% BSA, membranes were probed with primary antibodies to β-actin (8H10D10), p53 (7F5), PLC-γ (polyclonal), p-PLC-γ (polyclonal), Bcl-XL (54H6; all Cell Signaling), JNK (2C6), p-JNK (G9), Smad4 (polyclonal), p16 (polyclonal), c-Myc (9E10), CARD9 (polyclonal), Syk (polyclonal), p-Syk (polyclonal), Rb (C-15; all Cell Signalling), Dectin-1 (polyclonal; Abcam), Galectin-9 (polyclonal), and Dectin-1 Fc (fc-mdec1a; InvivoGen). Blots were developed by ECL (Thermo Scientific, Asheville, NC). RNA extraction was performed using the RNeasy Mini kit (Qiagen, Germantown, MD) as per manufacturer’s instructions. For Nanostring analysis, the nCounter mouse inflammation panel was employed using the nCounter Analysis System (both Nanostring, Seattle, Washington).