| Dimerization of profilin II upon binding the (GP5)3 peptide from VASP overcomes the inhibition of actin nucleation by profilin II and thymosin beta4. | |
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MedLine Citation:
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PMID: 10214957 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Profilin II dimers bind the (GP5)3 peptide derived from VASP with an affinity of approximately 0.5 microM. The resulting profilin II-peptide complex overcomes the combined capacity of thymosin beta4 and profilin II to inhibit actin nucleation and restores the extent of filament formation. We do not observe such an effect when barbed filament ends are capped. Neither can profilin I, in the presence of the peptide, promote actin polymerization during its early phase consistent with a lower affinity. Since a Pro17 peptide-profilin II complex only partially restores actin polymerization, the glycine residues in the VASP peptide appear important. |
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Authors:
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V Jonckheere; A Lambrechts; J Vandekerckhove; C Ampe |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: FEBS letters Volume: 447 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 1999 Mar |
Date Detail:
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Created Date: 1999-05-05 Completed Date: 1999-05-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 257-63 Citation Subset: IM |
Affiliation:
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Flanders Interuniversity Institute of Biotechnology, Department of Biochemistry, Faculty of Medicine, Universiteit Gent, Ghent, Belgium. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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chemistry*,
metabolism* Amino Acid Sequence Animals Cattle Cell Adhesion Molecules / chemistry*, metabolism* Contractile Proteins* Dimerization Microfilament Proteins / chemistry*, metabolism*, pharmacology Models, Molecular Molecular Sequence Data Peptide Fragments / chemistry, metabolism Phosphoproteins / chemistry*, metabolism* Profilins Protein Binding Protein Conformation Rabbits Thymosin / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Cell Adhesion Molecules; 0/Contractile Proteins; 0/Microfilament Proteins; 0/Peptide Fragments; 0/Phosphoproteins; 0/Profilins; 0/vasodilator-stimulated phosphoprotein; 61512-21-8/Thymosin; 77591-33-4/thymosin beta(4) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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