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• W2171480972 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." @default.
• W2171480972 created "2016-06-24" @default.
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• W2171480972 date "2003-11-10" @default.
• W2171480972 modified "2023-10-18" @default.
• W2171480972 title "LIME, a Novel Transmembrane Adaptor Protein, Associates with p56lck and Mediates T Cell Activation" @default.
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• W2171480972 doi "https://doi.org/10.1084/jem.20030232" @default.
• W2171480972 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2194117" @default.
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