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Cell Mol Life Sci. 2009 Sep;66(17):2949-52. doi: 10.1007/s00018-009-0071-x. Epub 2009 Jul 8.

TULA-family proteins: an odd couple.

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  • 1Department of Microbiology and Immunology, Sol Sherry Thrombosis Center and Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140, USA.


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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