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Identification and Characterization of the Actin-Binding Motif of Phostensin
Phostensin, a protein phosphatase 1 F-actin cytoskeleton-targeting subunit encoded by KIAA1949, consists of 165 amino acids and caps the pointed ends of actin filaments. Sequence alignment analyses suggest that the C-terminal region of phostensin, spanning residues 129 to 155, contains a consensus a...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546673/ https://www.ncbi.nlm.nih.gov/pubmed/23443105 http://dx.doi.org/10.3390/ijms131215967 |
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author | Wang, Tzu-Fan Lai, Ning-Sheng Huang, Kuang-Yung Huang, Hsien-Lu Lu, Ming-Chi Lin, Yu-Shan Chen, Chun-Yu Liu, Su-Qin Lin, Ta-Hsien Huang, Hsien-Bin |
author_facet | Wang, Tzu-Fan Lai, Ning-Sheng Huang, Kuang-Yung Huang, Hsien-Lu Lu, Ming-Chi Lin, Yu-Shan Chen, Chun-Yu Liu, Su-Qin Lin, Ta-Hsien Huang, Hsien-Bin |
author_sort | Wang, Tzu-Fan |
collection | PubMed |
description | Phostensin, a protein phosphatase 1 F-actin cytoskeleton-targeting subunit encoded by KIAA1949, consists of 165 amino acids and caps the pointed ends of actin filaments. Sequence alignment analyses suggest that the C-terminal region of phostensin, spanning residues 129 to 155, contains a consensus actin-binding motif. Here, we have verified the existence of an actin-binding motif in the C-terminal domain of phostensin using colocalization, F-actin co-sedimentation and single filament binding assays. Our data indicate that the N-terminal region of phostensin (1–129) cannot bind to actin filaments and cannot retard the pointed end elongation of gelsolin-actin seeds. Furthermore, the C-terminal region of phostensin (125–165) multiply bind to the sides of actin filaments and lacks the ability to block the pointed end elongation, suggesting that the actin-binding motif is located in the C-terminal region of the phostensin. Further analyses indicate that phostensin binding to the pointed end of actin filament requires N-terminal residues 35 to 51. These results suggest that phostensin might fold into a rigid structure, allowing the N-terminus to sterically hinder the binding of C-terminus to the sides of actin filament, thus rendering phostensin binding to the pointed ends of actin filaments. |
format | Online Article Text |
id | pubmed-3546673 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-35466732013-01-23 Identification and Characterization of the Actin-Binding Motif of Phostensin Wang, Tzu-Fan Lai, Ning-Sheng Huang, Kuang-Yung Huang, Hsien-Lu Lu, Ming-Chi Lin, Yu-Shan Chen, Chun-Yu Liu, Su-Qin Lin, Ta-Hsien Huang, Hsien-Bin Int J Mol Sci Article Phostensin, a protein phosphatase 1 F-actin cytoskeleton-targeting subunit encoded by KIAA1949, consists of 165 amino acids and caps the pointed ends of actin filaments. Sequence alignment analyses suggest that the C-terminal region of phostensin, spanning residues 129 to 155, contains a consensus actin-binding motif. Here, we have verified the existence of an actin-binding motif in the C-terminal domain of phostensin using colocalization, F-actin co-sedimentation and single filament binding assays. Our data indicate that the N-terminal region of phostensin (1–129) cannot bind to actin filaments and cannot retard the pointed end elongation of gelsolin-actin seeds. Furthermore, the C-terminal region of phostensin (125–165) multiply bind to the sides of actin filaments and lacks the ability to block the pointed end elongation, suggesting that the actin-binding motif is located in the C-terminal region of the phostensin. Further analyses indicate that phostensin binding to the pointed end of actin filament requires N-terminal residues 35 to 51. These results suggest that phostensin might fold into a rigid structure, allowing the N-terminus to sterically hinder the binding of C-terminus to the sides of actin filament, thus rendering phostensin binding to the pointed ends of actin filaments. Molecular Diversity Preservation International (MDPI) 2012-11-28 /pmc/articles/PMC3546673/ /pubmed/23443105 http://dx.doi.org/10.3390/ijms131215967 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Wang, Tzu-Fan Lai, Ning-Sheng Huang, Kuang-Yung Huang, Hsien-Lu Lu, Ming-Chi Lin, Yu-Shan Chen, Chun-Yu Liu, Su-Qin Lin, Ta-Hsien Huang, Hsien-Bin Identification and Characterization of the Actin-Binding Motif of Phostensin |
title | Identification and Characterization of the Actin-Binding Motif of Phostensin |
title_full | Identification and Characterization of the Actin-Binding Motif of Phostensin |
title_fullStr | Identification and Characterization of the Actin-Binding Motif of Phostensin |
title_full_unstemmed | Identification and Characterization of the Actin-Binding Motif of Phostensin |
title_short | Identification and Characterization of the Actin-Binding Motif of Phostensin |
title_sort | identification and characterization of the actin-binding motif of phostensin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546673/ https://www.ncbi.nlm.nih.gov/pubmed/23443105 http://dx.doi.org/10.3390/ijms131215967 |
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