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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

Tzu-Fan Wang ^1,† , Ning-Sheng Lai ^2,3,† , Kuang-Yung Huang ^2,3 , Hsien-Lu Huang ⁴ , Ming-Chi Lu ^2,3 , Yu-Shan Lin ¹ , Chun-Yu Chen ¹ , Su-Qin Liu ³ , Ta-Hsien Lin ^5,6,*  and Hsien-Bin Huang ^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; in revised form: 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

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