The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein.

Instituto de Biomedicina de Valencia (CSIC), Jaime Roig 11, 46010-Valencia, Spain.
In order to identify proteins that interact with Bmh2, a yeast member of the 14-3-3 protein family, we performed a two-hybrid screening using LexA-Bmh2 as bait. We identified Fin1, a novel intermediate filament protein, as the protein that showed the highest degree of interaction. We also identified components of the vesicular transport machinery such as Gic2 and Msb3, proteins involved in transcriptional regulation such as Mbf1, Gcr2 and Reg2, and a variety of other different proteins (Ppt1, Lre1, Rps0A and Ylr177w). We studied the interaction between Bmh2 and Fin1 in more detail and found that Bmh2 only interacted with phosphorylated forms of Fin1. In addition, we showed that Glc7, the catalytic subunit of the protein phosphatase 1 complex, was also able to interact with Fin1.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Base Sequence, Cytoskeletal Proteins, Fungal Proteins, Genes, Fungal, Molecular Sequence Data, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Plasmids, Protein Binding, Protein Phosphatase 1, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques
Biochem. J. Jul. 01, 2002; 365(0);51-6 [PUBMED:11931638]
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