Identification of a Leu-Ile internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor

被引：25

作者：

Thiel, S

Behrmann, I

Timmermann, A

Dahmen, H

Müller-Newen, G

Schaper, F

Tavernier, J

Pitard, V

Heinrich, PC

Graeve, L

机构：

[1] Rhein Westfal TH Aachen, Inst Biochem, D-52074 Aachen, Germany

[2] State Univ Ghent VIB, Dept Med Prot Chem, Mol Biol Unit, B-9000 Ghent, Belgium

[3] Univ Bordeaux 2, CNSR UMR 5540, F-33076 Bordeaux, France

来源：

BIOCHEMICAL JOURNAL | 1999年 / 339卷

关键词：

dileucine; endocytosis; gp130; interleukin-6; LIF receptor;

D O I：

10.1042/0264-6021:3390015

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：

Leukaemia inhibitory factor (LIF) signals via a heterodimeric receptor complex comprised of the LIF receptor (LIFR) and the interleukin (IL)-6 signal transducer gp130. Upon binding to its cognate receptor LIF is internalized. In this study, we show that the LIFR is endocytosed independently of gp130. By using a heterochimaeric receptor system we identified a dileucine-based internalization motif within the cytoplasmic domain of the LIFR. Our findings suggest that a heterodimeric LIFR/gp130 complex and homodimeric gp130/gp130 complex are endocytosed via distinct internalization signals.

引用

收藏

页码：15 / 19

页数：5

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