The β-thymosin enigma

Qiao Sun Hui; Helen L. Yin

doi:10.1196/annals.1415.021

The β-thymosin enigma

Qiao Sun Hui, Helen L. Yin

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

5 Scopus citations

Abstract

Actin dynamics in nonmuscle cells is controlled by the availability of actin nucleating sites and actin monomers. Thymosin β-4 (Tβ-4) has been implicated in modulating the availability of actin monomers in a large variety of cells. It together with actin nucleating, severing, and uncapping proteins, harnesses the intrinsic dynamic properties of actin to regulate the actin polymerization response in cells. Overexpression or addition of exogenous Tβ-4 or its homolog, Tβ-10, alters the actin cytoskeleton, and has multiple effects on cellular functions related to motility. Some of these effects are consistent with β-thymosins functioning exclusively as monomer-binding proteins, while others are not. Therefore, the complex pleiotropic effects of β-thymosin in cells may be due to direct and indirect effects on the actin cytoskeleton, as well as modulation of signaling pathways that will impact the cytoskeleton and a variety of cell functions.

Original language	English (US)
Title of host publication	Annals of the New York Academy of Sciences
Publisher	Blackwell Publishing Inc.
Pages	45-55
Number of pages	11
ISBN (Print)	1573317012, 9781573317016
DOIs	https://doi.org/10.1196/annals.1415.021
State	Published - Sep 2007

Publication series

Name	Annals of the New York Academy of Sciences
Volume	1112
ISSN (Print)	0077-8923
ISSN (Electronic)	1749-6632

Keywords

Actin
Cell migration
Integrin signaling
Thymosinβ-10
Thymosinβ-4

ASJC Scopus subject areas

General Neuroscience
General Biochemistry, Genetics and Molecular Biology
History and Philosophy of Science

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10.1196/annals.1415.021

Cite this

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title = "The β-thymosin enigma",

abstract = "Actin dynamics in nonmuscle cells is controlled by the availability of actin nucleating sites and actin monomers. Thymosin β-4 (Tβ-4) has been implicated in modulating the availability of actin monomers in a large variety of cells. It together with actin nucleating, severing, and uncapping proteins, harnesses the intrinsic dynamic properties of actin to regulate the actin polymerization response in cells. Overexpression or addition of exogenous Tβ-4 or its homolog, Tβ-10, alters the actin cytoskeleton, and has multiple effects on cellular functions related to motility. Some of these effects are consistent with β-thymosins functioning exclusively as monomer-binding proteins, while others are not. Therefore, the complex pleiotropic effects of β-thymosin in cells may be due to direct and indirect effects on the actin cytoskeleton, as well as modulation of signaling pathways that will impact the cytoskeleton and a variety of cell functions.",

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AU - Yin, Helen L.

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N2 - Actin dynamics in nonmuscle cells is controlled by the availability of actin nucleating sites and actin monomers. Thymosin β-4 (Tβ-4) has been implicated in modulating the availability of actin monomers in a large variety of cells. It together with actin nucleating, severing, and uncapping proteins, harnesses the intrinsic dynamic properties of actin to regulate the actin polymerization response in cells. Overexpression or addition of exogenous Tβ-4 or its homolog, Tβ-10, alters the actin cytoskeleton, and has multiple effects on cellular functions related to motility. Some of these effects are consistent with β-thymosins functioning exclusively as monomer-binding proteins, while others are not. Therefore, the complex pleiotropic effects of β-thymosin in cells may be due to direct and indirect effects on the actin cytoskeleton, as well as modulation of signaling pathways that will impact the cytoskeleton and a variety of cell functions.

AB - Actin dynamics in nonmuscle cells is controlled by the availability of actin nucleating sites and actin monomers. Thymosin β-4 (Tβ-4) has been implicated in modulating the availability of actin monomers in a large variety of cells. It together with actin nucleating, severing, and uncapping proteins, harnesses the intrinsic dynamic properties of actin to regulate the actin polymerization response in cells. Overexpression or addition of exogenous Tβ-4 or its homolog, Tβ-10, alters the actin cytoskeleton, and has multiple effects on cellular functions related to motility. Some of these effects are consistent with β-thymosins functioning exclusively as monomer-binding proteins, while others are not. Therefore, the complex pleiotropic effects of β-thymosin in cells may be due to direct and indirect effects on the actin cytoskeleton, as well as modulation of signaling pathways that will impact the cytoskeleton and a variety of cell functions.

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KW - Cell migration

KW - Integrin signaling

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KW - Thymosinβ-4

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ER -

The β-thymosin enigma

Abstract

Publication series

Keywords

ASJC Scopus subject areas

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