Abstract:
:Protein kinase C theta (PKC theta) is unique among PKC isozymes in its translocation to the center of the immune synapse in T cells and its unique downstream signaling. Here we show that the hematopoietic protein tyrosine phosphatase (HePTP) also accumulates in the immune synapse in a PKC theta-dependent manner upon antigen recognition by T cells and is phosphorylated by PKC theta at Ser-225, which is required for lipid raft translocation. Immune synapse translocation was completely absent in antigen-specific T cells from PKC theta-/- mice. In intact T cells, HePTP-S225A enhanced T-cell receptor (TCR)-induced NFAT/AP-1 transactivation, while the acidic substitution mutant was as efficient as wild-type HePTP. We conclude that HePTP is phosphorylated in the immune synapse by PKC theta and thereby targeted to lipid rafts to temper TCR signaling. This represents a novel mechanism for the active immune synapse recruitment and activation of a phosphatase in TCR signaling.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Nika K,Charvet C,Williams S,Tautz L,Bruckner S,Rahmouni S,Bottini N,Schoenberger SP,Baier G,Altman A,Mustelin Tdoi
10.1128/MCB.26.5.1806-1816.2006subject
Has Abstractpub_date
2006-03-01 00:00:00pages
1806-16issue
5eissn
0270-7306issn
1098-5549pii
26/5/1806journal_volume
26pub_type
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