Abstract
ADAMs (proteins containing A Disintegrin and A Metalloprotease domain) are multidomain and multifunctional proteins that are emerging as key regulators of critical events that occur at the cell surface. Many ADAMs (roughly half) are active metalloproteases, and several of these (e.g. ADAMs 10, 17, and 19) exert important functions in vivo, for example in development of the heart and brain. The best-characterized in vivo activity of ADAM proteases is as ectodomain sheddases. By shedding cell surface proteins (e.g. cytokines and growth factors), ADAMs initiate extracellular signaling events (e.g. signaling through epidermal growth factor receptors). ADAM-mediated ectodomain shedding (e.g. of Notch) can also set the stage for important intracellular signaling events. ADAMs have also been reported to shed surface proteins involved in both cell-cell and cell-matrix adhesion. The disintegrin and cysteine-rich domains of ADAMs exhibit adhesive activities in tissue culture-based studies. The important roles that several proteolytically inactive ADAMs play in development (ADAMs 2, 3, 14, and 23) suggest that ADAM adhesive activities may be relevant to their function. In this chapter, we first review the history and phylogeny of the ADAMs as well as structural and functional aspects of their major domains. We next review how ADAMs function as ectodomain sheddases, how their protease activities may be regulated, and how ADAMs may function in modulating cell adhesion and cell migration. We end with a very brief discussion of the role of ADAMs in development and disease and conclude by posing some questions for future research. Our goal is to give an appreciation for the widespread, varied, and fascinating means by which ADAMs affect, or may affect, key cell surface events: cell signaling, cell adhesion, and cell migration.
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References
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White, J., Bridges, L., DeSimone, D., Tomczuk, M., Wolfsberg, T. (2005). Introduction to the ADAM Family. In: Hooper, N.M., Lendeckel, U. (eds) The ADAM Family of Proteases. Proteases in Biology and Disease, vol 4. Springer, Boston, MA. https://doi.org/10.1007/0-387-25151-0_1
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