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  Polymerization of actin from the thymosin β4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1

Reichert, A. J. J., Heintz, D., Voelter, W. J., Mihelic−Rapp, M., & Faulstich, H. (1994). Polymerization of actin from the thymosin β4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1. FEBS Letters, 347(2), 247-250. doi:10.1016/0014-5793(94)00551-6.

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FEBSLett_347_1994_247.pdf (Any fulltext), 435KB
 
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 Creators:
Reichert, Andreas J. J.1, Author              
Heintz, Daniela2, Author              
Voelter, Wolfgang J., Author
Mihelic−Rapp, Mirna, Author
Faulstich, Heinz1, Author              
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1Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Actin polymerization; Thymosin β4; Actin nucleus; Myosin S1; Phalloidin
 Abstract: Thymosin β4 forms a 1:1 complex with actin and thereby prevents polymerization. Rapid formation of filaments from this complex was observed, however, when actin trimers were added. Polymerization can likewise be initiated by the addition of one equivalent of phalloidin or, less effectively, cytochalasin B. Since both toxins, which reportedly support nucleation, have similar effects as the covalently linked actin trimers, it appears that the formation of filaments from the actin—thymosin β4 complex depends on the availability of stable actin nuclei. Remarkably, rapid polymerization was also observed if small amounts of myosin S1 were added, suggesting that also myosin, a protein functionally connected with polymeric actin, can serve as a nucleation center. Considering the existence of thymosin β4 and related peptides in numerous mammalian tissues, our data suggest that spontaneous formation of microfilaments in non-muscle cells may be regulated at the level of nucleation. Uncontrolled polymerization induced by the formation of phalloidin-stabilized nuclei may explain the acute toxic effects of phalloidin in hepatocytes.

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Language(s): eng - English
 Dates: 1994-05-061994-05-232001-10-181994-06-27
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665129
DOI: 10.1016/0014-5793(94)00551-6
Other: 6940
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 347 (2) Sequence Number: - Start / End Page: 247 - 250 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501