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Updated: Jun 7, 2026

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
Published on: May 5, 2020
LIM domain protein FHL1B interacts with PP2A catalytic β subunit--a novel cell cycle regulatory pathway
Chi-Hang Wong1, Yin-Wan Wendy Fung, Enders Kai-On Ng
1School of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong.
Abstract:
Four-and-a-half LIM domain protein 1B (FHL1B) is an alternatively-spliced isoform of FHL1. In this study, FHL1B was demonstrated to interact with the β catalytic subunit (Cβ) of a type 2A protein phosphatase (PP2A) by yeast two-hybrid screening. Domain studies using a small-scale yeast two-hybrid interaction assay revealed the mediation of protein-protein interaction by FHL1B's C-terminus. Interaction between FHL1B and PP2A was further verified by co-immunoprecipitation. FHL1B was also shown to shuttle between nucleus and cytoplasm at different phases of the cell cycle. These data suggest that the FHL1B/PP2A(Cβ) interaction may illustrate a novel cell-cycle regulatory pathway.
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