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The interaction between E-tropomodulin and thymosin beta-10 rescues tumor cells from thymosin beta-10 mediated apoptosis by restoring actin architecture.
- Source :
-
FEBS letters [FEBS Lett] 2004 Jan 16; Vol. 557 (1-3), pp. 57-63. - Publication Year :
- 2004
-
Abstract
- Thymosin beta-10 (TB10) is a small G-actin binding protein that induces depolymerization of intracellular F-actin pools by sequestering actin monomers. Previously, we demonstrated that overexpression of TB10 in ovarian tumor cells increased the rate of cell death. As an initial step to define molecular mechanism of TB10-dependent apoptotic process in ovarian tumor cells, we searched a human ovary cDNA library for a novel TB10 binding protein using a yeast two-hybrid system. The selected protein was human E-tropomodulin (E-Tmod), another component of the actin binding proteins. Subsequently, two interacting protein components were determined quantitatively. Results showed that the full-length TB10 is required to bind with E-Tmod, and the TB10 binding site on E-Tmod partially overlaps with the actin binding site on E-Tmod. Moreover, introduction of E-Tmod cDNA into a tumor cell line reversed TB10 mediated apoptosis and restored actin architectures. These results may suggest that TB10 regulates apoptotic homeostasis by not only just binding to actin but also competing or blocking the protein complex formation of E-Tmod with actin.
- Subjects :
- Amino Acid Sequence
Binding Sites
Carrier Proteins chemistry
Carrier Proteins genetics
Cloning, Molecular
DNA, Complementary
Female
Gene Library
Humans
Molecular Sequence Data
Ovarian Neoplasms
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Thymosin chemistry
Thymosin genetics
Tropomodulin
Tumor Cells, Cultured
Actins chemistry
Actins metabolism
Apoptosis physiology
Carrier Proteins metabolism
Microfilament Proteins
Thymosin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 557
- Issue :
- 1-3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 14741341
- Full Text :
- https://doi.org/10.1016/s0014-5793(03)01438-8