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SOCS-6 negatively regulates T cell activation through targeting p56 lck to proteasomal degradation

Title
SOCS-6 negatively regulates T cell activation through targeting p56 lck to proteasomal degradation
Authors
Choi Y.B.Son M.Park M.Shin J.Yun G.
Ewha Authors
윤영대
SCOPUS Author ID
윤영대scopus
Issue Date
2010
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 285, no. 10, pp. 7271 - 7280
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The T cell-specific tyrosine kinase, p56lck, plays crucial roles in T cell receptor (TCR)-mediated T cell activation. Here, we report that SOCS-6 (suppressor of cytokine signaling-6) is a negative regulator of p56 lck. SOCS-6 was identified as a protein binding to the kinase domain of p56lck through yeast two-hybrid screening. SOCS-6 bound specifically to p56lck (F505), which mimics the active form of p56lck, but not to wild type p56lck. In Jurkat Tcells, SOCS-6 binding to p56lck was detected 1-2 h after TCR stimulation. Confocal microscopy showed that upon APC-T cell conjugation, SOCS-6 was recruited to the immunological synapse and colocalized with the active form of p56lck. SOCS-6 promoted p56lck ubiquitination and its subsequent targeting to the proteasome. Moreover, SOCS-6 overexpression led to repression of TCR-dependent interleukin-2 promoter activity. These results establish that SOCS-6 acts as a negative regulator of T cell activation by promoting ubiquitin-dependent proteolysis. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI
10.1074/jbc.M109.073726
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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