SAP-Regulated T Cell-APC Adhesion and Ligation-Dependent and   -Independent Ly108-CD3 zeta Interactions

doi:10.4049/jimmunol.1401660

CORC > 北京大学 > 生命科学学院

	SAP-Regulated T Cell-APC Adhesion and Ligation-Dependent and -Independent Ly108-CD3 zeta Interactions
	Chu, Coco ; Wang, Yifeng ; Zhang, Xu ; Ni, Xinya ; Cao, Junxia ; Xu, Wan ; Dong, Zhongjun ; Yuan, Pengfei ; Wei, Wensheng ; Ma, Yuanwu ; Zhang, Lianfeng ; Wu, Longyan ; Qi, Hai
刊名	journal of immunology
	2014
关键词	LINKED LYMPHOPROLIFERATIVE-DISEASE NATURAL-KILLER-CELLS GENE-PRODUCT SAP SLAM FAMILY RECEPTORS HUMORAL IMMUNITY B-CELLS SH2 DOMAIN LYMPH-NODES IMMUNOLOGICAL SYNAPSE TYROSINE-PHOSPHATASE
DOI	10.4049/jimmunol.1401660
英文摘要	The germinal center response requires cooperation between Ag-specific T and B lymphocytes, which takes the form of long-lasting cell-cell conjugation in vivo. Signaling lymphocytic activation molecule (SLAM)-associated protein (SAP) is required for stable cognate T-B cell conjugation, whereas SLAM family transmembrane (TM) receptor Ly108 may negatively regulate this process. We show that, other than phosphotyrosine-binding, SAP does not harbor motifs that recruit additional signaling intermediates to stabilize T-B adhesion. Ly108 dampens T cell adhesion to not only Ag-presenting B cells, but also dendritic cells by inhibiting CD3 zeta phosphorylation through two levels of regulated Ly108-CD3 zeta interactions. Constitutively associated with Src homology 2 domain-containing tyrosine phosphatase-1 even in SAP-competent cells, Ly108 is codistributed with the CD3 complex within a length scale of 100-200 nm on quiescent cells and can reduce CD3 zeta phosphorylation in the absence of overt TCR stimulation or Ly108 ligation. When Ly108 is engaged in trans during cell-cell interactions, Ly108-CD3 zeta interactions are promoted in a manner that uniquely depends on Ly108 TM domain, leading to more efficient CD3 zeta dephosphorylation. Whereas replacement of the Ly108 TM domain still allows the constitutive, colocalization-dependent inhibition of CD3 zeta phosphorylation, it abrogates the ligation-dependent Ly108-CD3 zeta interactions and CD3 zeta dephosphorylation, and it abolishes the suppression on Ag-triggered T-B adhesion. These results offer new insights into how SAP and Ly108 antagonistically modulate the strength of proximal TCR signaling and thereby control cognate T cell-APC interactions.; Immunology; SCI(E); PubMed; 1; ARTICLE; qihai@tsinghua.edu.cn; 8; 3860-3871; 193
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/342220]
专题	生命科学学院
推荐引用方式 GB/T 7714	Chu, Coco,Wang, Yifeng,Zhang, Xu,et al. SAP-Regulated T Cell-APC Adhesion and Ligation-Dependent and -Independent Ly108-CD3 zeta Interactions[J]. journal of immunology,2014.
APA	Chu, Coco.,Wang, Yifeng.,Zhang, Xu.,Ni, Xinya.,Cao, Junxia.,...&Qi, Hai.(2014).SAP-Regulated T Cell-APC Adhesion and Ligation-Dependent and -Independent Ly108-CD3 zeta Interactions.journal of immunology.
MLA	Chu, Coco,et al."SAP-Regulated T Cell-APC Adhesion and Ligation-Dependent and -Independent Ly108-CD3 zeta Interactions".journal of immunology (2014).