Evidence map›Paper›PMID 24434620›Full record

ArticleInternational journal of molecular sciences2014

Identification of the high molecular weight isoform of phostensin.

Yu-Shan Lin, Hsien-Lu Huang, Wei-Ting Liu, Ta-Hsien Lin, Hsien-Bin Huang

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Yu-Shan LinDepartment of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. lambdaphagecarol@yahoo.com.tw.
Hsien-Lu HuangDepartment of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. estrus@mail2000.com.tw.
Wei-Ting LiuDepartment of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. weiting0608@hotmail.com.
Ta-Hsien LinDepartment of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. thlin@vghtpe.gov.tw.
Hsien-Bin HuangDepartment of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 62102, Taiwan. biohbh@ccu.edu.tw.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

ActinsAmino Acid SequenceBase SequenceHEK293 CellsHumansJurkat CellsMolecular Sequence DataMolecular WeightProtein BindingProtein IsoformsProtein Phosphatase 1RNA, MessengerActinsPPP1R18 protein, humanProtein IsoformsProtein Phosphatase 1RNA, Messenger

Identifiers

PMID24434620
PMCPMC3907856

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