TULA-family proteins: an odd couple |
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Authors: | Alexander Y Tsygankov |
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Institution: | (1) Department of Microbiology and Immunology, Sol Sherry Thrombosis Center and Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, 3400 N. Broad Street, Philadelphia, PA 19140, USA |
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Abstract: | Two members of the TULA family (TULA/STS-2/UBASH3A and TULA-2/STS-1/UBASH3B) recently emerged as novel regulators of several
cellular functions. The degree of structural similarity between the TULA-family proteins is typical for proteins that belong
to the same family. Furthermore, the experiments with knockout mice lacking these proteins may be interpreted as suggesting
that functions of TULA-family proteins in T lymphocytes overlap. At the same time, TULA and TULA-2 exhibit clear functional
dissimilarities, starting with the finding that a conserved phosphatase domain present in both proteins exhibits remarkable
differences in enzymatic activity; TULA-2 is an active phosphatase capable of dephosphorylating multiple tyrosine-phosphorylated
proteins, whereas the phosphatase activity of TULA is extremely low. In contrast, TULA, but not TULA-2, facilitates growth
factor withdrawal-induced apoptosis in T cells. In spite of their apparent importance, the functional role of TULA-family
proteins is not well understood. In particular, the role of functional dissimilarities between them remains unclear. |
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Keywords: | TULA STS UBASH3 Ubiquitin Phosphatase |
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