CK2-dependent C-terminal phosphorylation at T300 directs the nuclear transport of TSPY protein.

TSPY (testis-specific protein, Y-encoded) is a member of the greater SET/NAP family of molecules with various functions, e.g., in chromatin remodeling, regulation of gene expression, and has been implicated to play a role in the malignant development of gonadoblastoma, testicular and prostate cancer. Here we demonstrate that the C-terminus has ...
a functional role for the nucleo-cytoplasmatic shuttling of the TSPY protein. Using various combinations of in vitro mutagenesis and enhanced green fluorescent protein reporter gene-expression experiments we were able to show that while the deletion of C-terminus leads to a decreased stability and enhanced degradation of the protein, the selective mutation of a C-terminal CK2 phosphorylation site (T300) prevents the TSPY protein from entering the nucleus. We conclude that phosphorylation of the (T300) residue is a necessary and functional prerequisite for TSPY's transport into the nucleus reminding of comparable data from a related Drosophila molecule, NAP1.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Casein Kinase II, Cell Cycle Proteins, Cell Line, Cell Line, Tumor, Cell Nucleus, Chromatin, Cytoplasm, DNA Mutational Analysis, DNA Primers, Drosophila, Gene Deletion, Gene Expression Regulation, Green Fluorescent Proteins, Humans, Immunoblotting, Molecular Sequence Data, Mutagenesis, Mutation, Mutation, Missense, Phosphorylation, Protein Structure, Tertiary, Recombinant Fusion Proteins, Time Factors
Biochem. Biophys. Res. Commun.
Date: Mar. 10, 2006
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