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Int. J. Mol. Sci. 2012, 13(12), 15967-15982; doi:10.3390/ijms131215967
Article

Identification and Characterization of the Actin-Binding Motif of Phostensin

1,†
, 2,3,†
, 2,3
, 4
, 2,3
, 1
, 1
, 3
, 5,6,*  and 1,*
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 These authors contributed equally to this work.
* Authors to whom correspondence should be addressed.
Received: 20 September 2012 / Revised: 15 November 2012 / Accepted: 19 November 2012 / Published: 28 November 2012
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract

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.
Keywords: phostensin; actin filament; KIAA1949; protein phosphatase phostensin; actin filament; KIAA1949; protein phosphatase
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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