The {beta}-Thymosin Enigma

doi:10.1196/annals.1415.021

Ann. N.Y. Acad. Sci., Annals PrePrint, published online ahead of print May 10, 2007
doi: 10.1196/annals.1415.021
Copyright © 2007 by the New York Academy of Sciences
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The ${beta}$ -Thymosin Enigma

Hui-Qiao Sun ¹ Helen L. Yin ²^*

¹ Physiology, UT Southwestern Medical Center, Dallas, Texas, United States
² Physiology, UT Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas, 75390-9040, United States

^* To whom correspondence should be addressed. E-mail: helen.yin{at}utsouthwestern.edu.

PrePrint Abstract

ABSTRACT: Actin dynamics in nonmuscle cells is controlled bythe availability of actin nucleating sites and actin monomers. Thymosin ${beta}$ 4 (T ${beta}$ 4) have been implicated in modulating the availabilityof actin monomers in a large variety of cells. It, togetherwith actin nucleating, severing and uncapping proteins harnessthe intrinsic dynamic properties of actin to regulate the actinpolymerization response in cells. Overexpression or additionof exogenous T ${beta}$ 4 or its homolog, T ${beta}$ 10, alters the actin cytoskeleton,and has multiple effects on cellular functions related to cellmotility. Some of these effects are consistent with ${beta}$ -thymosinsfunctioning exclusively as monomer binding proteins, while othersare not. Therefore, the complex pleiotropic effects of ${beta}$ -thymosinin cells may be due to direct and indirect effects on the actincytoskeleton, as well as modulation of signaling pathways thatwill impact the cytoskeleton and a variety of cell functions.

Key Words: thymosin ß4, thymosin ß10, actin, cell migration, integrin, signaling