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Histones are highly conserved proteins that function in the organization of nuclear DNA to create chromatin in eukaryotic cells. Post-translational alterations of histones are critical to monitoring and regulating DNA structure, expression, and gene transcription.

The TARDBP gene codes for a transcriptional repressor protein known as TDP-43. The protein encoded by the TARDBP gene binds TAR DNA and functions to regulate translation. TDP-43 can also bind RNA which leads to transcriptional repression and the formation of splice variants encoding alternate forms of proteins. Additionally, the TARDBP gene plays an important role in mRNA transport.

Adipose differentiation-related protein (ADFP; also known as ADRP or adipophilin), is a lipid droplet protein found in most cells and tissues. These lipids droplets may serve as local energy reserves or sources of lipid for membrane synthesis. Furthermore, they may protect cells from the harmful effects of excess lipid accumulation by sequestering toxic lipid species away from pathways leading to cell death (1). ADFP expression is strongly induced in cells with increased lipid load.

TRPV1 (transient receptor potential cation channel subfamily vanilloid member type 1) is a polymodal nociceptor that is commonly expressed in peripheral nerve endings and dorsal root ganglia. It is activated by heat, low pH, vanilloids, capsaicin, and other noxious stimuli and is involved in the transmission and modulation of pain. Not surprisingly, TRPV1 is directly related to hyperalgesia—increased sensitivity to pain—as hyperalgesia is significantly reduced when TRPV1 is genetically eliminated or pharmacologically blocked.

ABCG1 (ATP-binding cassette sub-family G member 1) is a transporter protein that is primarily involved in macrophage lipid homeostasis. It is a member of the superfamily of ATP-binding cassette (ABC) transporters and localizes to intracellular compartments associated with endoplasmic reticulum and golgi membranes.

p62/SQSTM1 (sequestosome 1) is ubiquitously-expressed cytoplasmic/adaptor protein. SQSTM1 functions as a signaling hub for various signal transduction pathways involved in apoptosis, cell differentiation, apoptosis, immune response, and K+ channel regulation. It is conserved in vertebrates and can be induced by a wide variety of triggers including the proteasomal inhibitor PSI, PGJ2/prostaglandin J2, and the tumor promoting agent phorbol 12-myristate 13-acetate (PMA).

The extracellular matrix (ECM) is a well-structured composite of collagens, proteoglycans, glycoproteins, and growth factors proficient of generating variable measures of tissue tensile potency, from mucosal linings to bones. ECM predominantly comprises the cellular milieu outside the circulation and is established as having a major regulatory effect on cell activity.  There has been a considerable amount of attention towards the disparate conditions in which ECM unambiguously sends or alters signals to the surrounding cells.

Hematopoiesis is a complicated process that is controlled by both intrinsic and extrinsic cellular factors. It is a process of progression by which the diverse cell pedigrees that develop the blood and immune system are spawned from a shared pluripotent hematopoietic stem cell (HSC). Throughout the lifespan of an adult, two distinct hematopoietic systems are present, both resulting through embryonic development but only one of them enduring into adulthood.

The Lin28-Let-7 stem cell differentiation regulatory pathway is responsible for maintaining stem cell pluripotency. Specifically, Lin28 causes uridiylation of the let-7 miRNA precursor, which prevents differentiation processing by Dicer. Instead, the Uridylated let-7 is degraded by a previously unidentified exonuclease protein. In the article “A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7 pathway” HM Chang, et al.

The biological importance of protein phosphorylation is underlined by the existence of 500 or more protein kinases within the human genome. In most cases, phosphorylation of serine residues creates binding surfaces for a variety of phospho-amino acid binding proteins. Phosphorylation is a key post-translational modification necessary for normal cell signaling and is a key player in cellular function. Phosphorylated proteins mediate cell division, differentiation, signal transduction and other key cell signaling processes.