Difference between revisions of "Phosphatase Subfamily STS"
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=== Functions === | === Functions === | ||
| − | Human STS-1 and STS-2 are involved in T Cell Receptor | + | Human STS-1 and STS-2 are involved in T Cell Receptor (TCR) signaling pathways by regulating kinase Syk and ZAP-70, two members of Syk kinase subfamily. STS-2 is predominantly in naive and mature T cells , whereas STS-1 is expressed ubiquitously. |
| − | STS-1 decreases tyrosine phosphorylation of Syk ''in vivo'' and ''in vitro'' <cite>chen10, carpino04</cite>. Inactivated STS-1 increases tyrosine phosphorylation of Syk in cells co-transfected to overexpress these proteins, thus acting as a dominant-negative form that suppresses dephosphorylation of Syk caused by endogenous STS-1. However, the same assay on STS-2 shows the phosphatase activity of STS-2 is negligible compared to STS-1 <cite>STS_2</cite>. In addition, both STS-1 and STS-2 regulates kinase ZAP-70 activation <cite>carpino04</cite>. | + | STS-1 decreases tyrosine phosphorylation of Syk ''in vivo'' and ''in vitro'' <cite>chen10, carpino04</cite>. Inactivated STS-1 increases tyrosine phosphorylation of Syk in cells co-transfected to overexpress these proteins, thus acting as a dominant-negative form that suppresses dephosphorylation of Syk caused by endogenous STS-1. However, the same assay on STS-2 shows the phosphatase activity of STS-2 is negligible compared to STS-1. The UBA domain of STS-2 and SH3-dependent Cbl-binding are required for this function <cite>STS_2</cite>. In addition, both STS-1 and STS-2 regulates kinase ZAP-70 activation <cite>carpino04</cite>. |
| − | Human STS-1 can also dephosphorylate phospho-tyrosines on EGFR. The histidine phosphatase domain of STS-1, but not of STS-2, dephosphorylates the EGFR at multiple tyrosines, and thereby terminating its signalling and endocytosis <cite>STS_1</cite> | + | Human STS-1 can also dephosphorylate phospho-tyrosines on EGFR. The histidine phosphatase domain of STS-1, but not of STS-2, dephosphorylates the EGFR at multiple tyrosines, and thereby terminating its signalling and endocytosis <cite>STS_1</cite>. |
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===References=== | ===References=== | ||
Revision as of 04:50, 3 January 2015
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): HP, branch1 family: Subfamily STS
Contents
Evolution
STS subfamily is found in most metazoan. Human has two STSs: STS-1 (TULA-2 or UBASH3B) and STS-2 (TULA-1 or UBASH3A). STS-2 is present in lobe-finned fish, birds and mammals, but not other bony fishes. STS-1 emerged earlier than STS-2, which is found in most metazoan, from sponge to nematodes, insects, fishes, birds, and mammals.
Domain
STS has three domains: UBA, SH3 and HP2 phosphatase domain.
Functions
Human STS-1 and STS-2 are involved in T Cell Receptor (TCR) signaling pathways by regulating kinase Syk and ZAP-70, two members of Syk kinase subfamily. STS-2 is predominantly in naive and mature T cells , whereas STS-1 is expressed ubiquitously.
STS-1 decreases tyrosine phosphorylation of Syk in vivo and in vitro [1, 2]. Inactivated STS-1 increases tyrosine phosphorylation of Syk in cells co-transfected to overexpress these proteins, thus acting as a dominant-negative form that suppresses dephosphorylation of Syk caused by endogenous STS-1. However, the same assay on STS-2 shows the phosphatase activity of STS-2 is negligible compared to STS-1. The UBA domain of STS-2 and SH3-dependent Cbl-binding are required for this function [3]. In addition, both STS-1 and STS-2 regulates kinase ZAP-70 activation [2].
Human STS-1 can also dephosphorylate phospho-tyrosines on EGFR. The histidine phosphatase domain of STS-1, but not of STS-2, dephosphorylates the EGFR at multiple tyrosines, and thereby terminating its signalling and endocytosis [4].
References
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