RANK (Fc-Fusion)

RANK (for receptor activator of NF-kappaB), a type I membrane protein, is a member of the TNFR superfamily and plays important roles in bone physiology as well as in regulation of the interactions between dendritic cells and T lymphocytes.

Interacting protein(s): RANKL
Related products: TNF-Receptor Superfamily

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Quick Specs

Description

RANK (for receptor activator of NF-kappaB), a type I membrane protein, is a member of the TNFR superfamily and plays important roles in bone physiology as well as in regulation of the interactions between dendritic cells and T lymphocytes. RANK is ubiquitously expressed at high levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. Ligand of RANK, RANKL, also called osteoclast differentiation factor (ODF), binds to both RANK on cell surface and the soluble decoy receptor osteoprotegerin (OPG).

The balance between the surface RANK-mediated osteoclastogenesis and the decoy OPG-mediated inhibition fine tunes the activity of osteoclasts that ultimately controls the bone remodeling. Defects in RANK are the cause of a variety of osteo-disorders including familial expansile osteolysis (FEO); Paget disease of bone type 2 (PDB2) and osteopetrosis autosomal recessive type 7 (OPTB7). OPTB7 also called osteoclast-poor osteopetrosis with hypogammaglobulinemia. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone.

The disorder occurs in two forms: a severe autosomal recessive form with an infancy onset, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTB7 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development.

Amino Acid Sequence.

References

1. Yao Z, Getting SJ, Locke IC. Regulation of TNF-Induced Osteoclast Differentiation. Cells. 2021;11(1). Epub 20211231. doi: 10.3390/cells11010132. PubMed PMID: 35011694; PubMed Central PMCID: PMC8750957.

2. A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function. Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C., Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L. Nature 390:175-179 (1997)

3. RANK is the essential signaling receptor for osteoclast differentiation factor in osteoclastogenesis. Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K., Morinaga T., Higashio K. Biochem. Biophys. Res. Commun. 253:395-400 (1998)

4. Mutations in TNFRSF11A, affecting the signal peptide of RANK, cause familial expansile osteolysis."

5. Hughes A.E., Ralston S.H., Marken J., Bell C., MacPherson H., Wallace R.G.H., van Hul W., Whyte M.P., Nakatsuka K., Hovy L., Anderson D.M. Nat. Genet. 24:45-48 (2000)

6. Human osteoclast-poor osteopetrosis with hypogammaglobulinemia due to TNFRSF11A (RANK) mutations. Guerrini M.M., Sobacchi C., Cassani B., Abinun M., Kilic S.S., Pangrazio A., Moratto D., Mazzolari E., Clayton-Smith J., Orchard P., Coxon F.P., Helfrich M.H., Crockett J.C., Mellis D., Vellodi A., Tezcan I., Notarangelo L.D., Rogers M.J. expand/collapse author list Frattini A. Am. J. Hum. Genet. 83:64-76 (2008)