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Open AccessArticle

Identification and Characterization of the Actin-Binding Motif of Phostensin

1
Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan
2
College of Medicine, Tzu-Chi University, Hualien 97004, Taiwan
3
Section of Allergy, Immunology and Rheumatology, Department of Medicine, DaLin Tzu Chi Buddhist Hospital, Chia-Yi 62247, Taiwan
4
Department of Nutrition and Health Science, Fooyin University, Kaohsiung 83102, Taiwan
5
Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan
6
Department of Medical Research & Education, Taipei Veterans General Hospital, Taipei 11217, Taiwan
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2012, 13(12), 15967-15982; https://doi.org/10.3390/ijms131215967
Received: 20 September 2012 / Revised: 15 November 2012 / Accepted: 19 November 2012 / Published: 28 November 2012
(This article belongs to the Section Biochemistry)
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. View Full-Text
Keywords: phostensin; actin filament; KIAA1949; protein phosphatase phostensin; actin filament; KIAA1949; protein phosphatase
MDPI and ACS Style

Wang, T.-F.; Lai, N.-S.; Huang, K.-Y.; Huang, H.-L.; Lu, M.-C.; Lin, Y.-S.; Chen, C.-Y.; Liu, S.-Q.; Lin, T.-H.; Huang, H.-B. Identification and Characterization of the Actin-Binding Motif of Phostensin. Int. J. Mol. Sci. 2012, 13, 15967-15982.

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