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Int. J. Mol. Sci. 2014, 15(1), 1068-1079; doi:10.3390/ijms15011068
Communication

Identification of the High Molecular Weight Isoform of Phostensin

1,†
,
2,†
,
1
,
3,4,*  and 1,*
1 Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan 2 Department of Nutrition and Health Science, Fooyin University, Kaohsiung 83102, Taiwan 3 Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan 4 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: 11 December 2013 / Revised: 31 December 2013 / Accepted: 6 January 2014 / Published: 15 January 2014
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract

Phostensin is encoded by KIAA1949. 5'-RACEanalysis has been used to identify the translation start site of phostensin mRNA, indicating that it encodes 165 amino acids with an apparent molecular weight of 26 kDa on SDS-PAGE. This low-molecular-weight phostensin is present in human peripheral blood mononuclear cells and many leukemic cell lines. Phostensin is a protein phosphatase-1(PP1) binding protein. It also contains one actin-binding motif at its C-terminal region and binds to the pointed ends of actin filaments, modulating actin dynamics. In the current study, a high-molecular-weight phostensin is identified by using immunoprecipitationin combination with a proteomic approach. This new species of phostensin is also encoded by KIAA1949 and consists of 613 amino acids with an apparent molecular weight of 110 kDa on SDS-PAGE. The low-molecular-weight and high-molecular-weight phostensins were named as phostensin-α and phostensin-β, respectively. Although phostensin-α is the C-terminal region of phostensin-β, it is not degraded from phostensin-β. Phostensin-β is capable of associating with PP1 and actin filaments, and is present in many cell lines.
Keywords: phostensin-α; phostensin-β; KIAA1949; protein phosphatase-1; actin-binding protein phostensin-α; phostensin-β; KIAA1949; protein phosphatase-1; actin-binding protein
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Lin, Y.-S.; Huang, H.-L.; Liu, W.-T.; Lin, T.-H.; Huang, H.-B. Identification of the High Molecular Weight Isoform of Phostensin. Int. J. Mol. Sci. 2014, 15, 1068-1079.

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