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c-Myc is a protein of the Myc family of transcription factors (c-Myc, B-Myc, L-Myc, N-Myc, and s-Myc) encoded by the MYC proto-oncogene. c-Myc was first discovered as the cellular homolog of the retroviral v-Myc oncogene. c-Myc is a transcription factor for genes involved in cell growth, proliferation, differentiation, and apoptosis. c-Myc contains a basic helix-loop-helix domain and a leucine zipper domain that allow for its heterodimerization with its binding partner Max. Myc/Max complexes are able to activate genes via the Myc transactivation domain (1).

Caspases are a family of cysteine-aspartic acid proteases that are responsible for the initiation and execution of apoptosis. Caspase-8 is a 55 kDa protein expressed as an inactive procaspase that resides in the cytosol. Activation of Caspase-8 requires cleavage into its large (17-21 kDa) and small (10-13 kDa) catalytic subunits. Caspase-8 has been shown to play a role in the induction of apoptosis by both death receptor mediated and non-receptor mediated mechanisms (1). Caspase-8 signals to effector Caspase-3 to execute apoptosis.

Matrix metalloproteinases (MMPs) are responsible for the degradation of extracellular matrix proteins. MMPs are essential for tissue remodeling during normal processes such as embryonic development as well as pathological conditions such as arthritis and tumor metastasis. MMP3, a member of the stromelysin family, has broad specificity for proteins such as collagens, fibronectin, proteoglycans, and elastin making it an important player in extracellular matrix remodeling. These activities are especially important during tumorigenesis by enhancing epithelial to mesenchymal transition.

The vertebrate fibroblast growth factor receptor (FGFR) family is an important group of proteins involved in embryonic development and the growth and proliferation of adult cells. Mutations in FGFR proteins can lead to pathologies including bone or limb defects and various forms of cancer. FGFR proteins are receptor tyrosine kinases that, upon ligand binding, dimerize and signal through the MAPK and PLCγ pathways.

Calnexin is an abundant 90kDa chaperone protein that resides in the membrane of the endoplasmic reticulum. Calnexin and the related calreticulin protein function together to ensure the proper folding of glycoproteins. By binding to partially folded or misfolded proteins, Calnexin functions as an important quality control monitor ensuring proper folding of proteins destined for the plasma membrane or secretion.