Cytoplasmic domain of E-selectin contains a non-tyrosine endocytosis signal

被引:17
作者
Chuang, PI
Young, BA
Thiagarajan, RR
Cornejo, C
Winn, RK
Harlan, JM
机构
[1] UNIV WASHINGTON,DEPT PEDIAT,SEATTLE,WA 98195
[2] UNIV WASHINGTON,DEPT SURG,SEATTLE,WA 98195
关键词
D O I
10.1074/jbc.272.40.24813
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
E-selectin is an activation-dependent, endothelial cell-restricted adhesion molecule that is internalized and degraded rapidly once expressed on the cell surface. Tyrosine-containing structural motifs play an important role in the internalization of a number of integral proteins, and the membrane-proximal E-selectin cytoplasmic tyrosine residue (Tyr(582)) conforms to the endocytosis motif proposed previously, To determine the endocytosis motif in E-selectin, we selectively introduced truncation, substitution and deletion mutations to the cytoplasmic tail of E-selectin. We analyzed the internalization kinetics of surface-expressed wild-type and mutant E-selectin constructs in transiently transfected Chinese hamster ovary cells using I-125-labeled E-selectin monoclonal antibody (I-126-P6E2) in an acid elution assay. Interestingly, truncation immediately membrane proximal to Tyr(582) (Delta DGS construct) did not alter internalization kinetics significantly (Delta DGS versus wild-type, mean surface half-life = 42 versus 45 min, respectively). Thus, it appears that the tyrosine residues are not required for internalization of E-selectin. Additional analyses indicated that Ser(581) was necessary but alone was insufficient for surface E-selectin endocytosis. Thus, we conclude that there exists a novel non-tyrosine-containing endocytosis signal in the cytoplasmic tail which in volves Ser(581) and residues membrane-proximal to it.
引用
收藏
页码:24813 / 24818
页数:6
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