Key result
FHL1B interacts with the beta catalytic subunit of PP2A via its C-terminus and shuttles between the nucleus and cytoplasm, suggesting a novel cell-cycle regulatory pathway.
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Hypothesis-generating for cell-cycle control in muscle cells; leaves open relevance to cardiac proliferation or disease.
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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Wong et al. (2010) studied this question. FHL1B interacts with the beta catalytic subunit of PP2A via its C-terminus and shuttles between the nucleus and cytoplasm, suggesting a novel cell-cycle regulatory pathway.
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