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Regulation of T cell development by the deubiquitinating enzyme CYLD
Abstract
T cell receptor signaling is essential for the generation and maturation of T lymphocyte precursors. Here we identify the deubiquitinating enzyme CYLD as a positive regulator of proximal T cell receptor signaling in thymocytes. CYLD physically interacted with active Lck and promoted recruitment of active Lck to its substrate, Zap70. CYLD also removed both Lys 48- and Lys 63-linked polyubiquitin chains from Lck. Because of a cell-autonomous defect in T cell development, CYLD-deficient mice had substantially fewer mature CD4(+) and CD8(+) single-positive thymocytes and peripheral T cells.
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CYLD has an essential role in T-cell development.
“Analysis of these mice instead demonstrated an essential role for CYLD in T-cell development (47)”
From Essential Role of Ubiquitin-Specific Protease 8 for Receptor Tyrosine Kinase Stability and Endocytic Trafficking In Vivo (2007) · cites this paper as [47]
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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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Self-citation
Metadata
- Authors
- Reiley, W. W., Zhang, M., Jin, W., Losiewicz, M., Donohue, K. B., Norbury, C. C., & Sun, S.-C.
- Venue
- Nature Immunology
- Published
- 2006-02-26
- Volume
- 7
- Issue
- 4
- Pages
- 411-417
- ISSN
- 1529-2908
- 1529-2916
- Cited by
- 198
- References
- 2
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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