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LIME, a Novel Transmembrane Adaptor Protein, Associates with p56 lck and Mediates T Cell Activation

Title
LIME, a Novel Transmembrane Adaptor Protein, Associates with p56 lck and Mediates T Cell Activation
Authors
Hur E.M.Son M.Lee O.-H.Choi Y.B.Park C.Lee H.Yun Y.
Ewha Authors
윤영대
SCOPUS Author ID
윤영대scopus
Issue Date
2003
Journal Title
Journal of Experimental Medicine
ISSN
0022-1007JCR Link
Citation
vol. 198, no. 10, pp. 1463 - 1473
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
In this study, we identify and characterize a novel transmembrane adaptor protein, designated Lck-interacting membrane protein (LIME), as a binding partner of the Lck Src homology (SH)2 domain. LIME possesses a short extracellular domain, a transmembrane domain, and a cytoplasmic tail containing five tyrosine-based motifs. The protein is primarily expressed in hematopoietic cells and lung. Interestingly, LIME expression is up-regulated by TCR stimulation and sustained up to 24 h, suggesting that LIME acts throughout the early to late stages of T cell activation. LIME is localized to membrane rafts and distributed within the T cell-APC contact site. Upon TCR stimulation of Jurkat T cells, LIME associates with Lck as a tyrosine-phosphorylated protein. Experiments using Jurkat T cells expressing CD8-LIME chimera reveal that the protein associates with phosphatidylinositol 3-kinase, Grb2, Gads, and SHP2, and activates ERK1/2 and JNK but not p38. Moreover, overexpression of LIME in Jurkat T cells induces transcriptional activation of the IL-2 promoter. Our data collectively show that LIME is a raft-associated transmembrane adaptor protein linking TCR stimuli to downstream signaling pathways via associations with Lck.
DOI
10.1084/jem.20030232
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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