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Identification of the high molecular weight isoform of phostensin.
Lin, Yu-Shan; Huang, Hsien-Lu; Liu, Wei-Ting; Lin, Ta-Hsien; Huang, Hsien-Bin.
Afiliação
  • Lin YS; Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. lambdaphagecarol@yahoo.com.tw.
  • Huang HL; Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. estrus@mail2000.com.tw.
  • Liu WT; Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. weiting0608@hotmail.com.
  • Lin TH; Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. thlin@vghtpe.gov.tw.
  • Huang HB; Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. biohbh@ccu.edu.tw.
Int J Mol Sci ; 15(1): 1068-79, 2014 Jan 15.
Article em En | MEDLINE | ID: mdl-24434620
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-ß, respectively. Although phostensin-α is the C-terminal region of phostensin-ß, it is not degraded from phostensin-ß. Phostensin-ß is capable of associating with PP1 and actin filaments, and is present in many cell lines.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteína Fosfatase 1 Tipo de estudo: Diagnostic_studies Limite: Humans Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteína Fosfatase 1 Tipo de estudo: Diagnostic_studies Limite: Humans Idioma: En Ano de publicação: 2014 Tipo de documento: Article