CK2-dependent C-terminal phosphorylation at T{sup 30} directs the nuclear transport of TSPY protein
- Institute of Human Genetics, Johann Wolfgang GoeUniversity Hospital, Frankfurt (Germany)
- Institute of Pharmacology and Toxicology, Johann Wolfgang GoeUniversity Hospital, Frankfurt (Germany)
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 (T{sup 30}) prevents the TSPY protein from entering the nucleus. We conclude that phosphorylation of the (T{sup 30}) residue is a necessary and functional prerequisite for TSPY's transport into the nucleus reminding of comparable data from a related Drosophila molecule, NAP1.
- OSTI ID:
- 20798827
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 341, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2005.12.190; PII: S0006-291X(06)00022-2; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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