Constitutive internalization and association with adaptor protein-2 of theinterleukin-6 signal transducer gp130

Citation
S. Thiel et al., Constitutive internalization and association with adaptor protein-2 of theinterleukin-6 signal transducer gp130, FEBS LETTER, 441(2), 1998, pp. 231-234
Citations number
25
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
441
Issue
2
Year of publication
1998
Pages
231 - 234
Database
ISI
SICI code
0014-5793(199812)441:2<231:CIAAWA>2.0.ZU;2-O
Abstract
The transmembrane protein gp130 is the common signalling receptor subunit f or the interleukin-6 (IL-6)-type cytokines, It has recently been shown that the cytoplasmic domain of gp130 contains a dileucine internalization motif and that endocytosis of gp130 occurs signal-independent. Here, we have stu died whether gp130 itself undergoes constitutive internalization or whether its endocytosis is stimulated by formation of the IL-6/IL-6R/gp130 complex . Using two different assays, we found that gp130 is internalized independe nt from lL-6/IL-6R stimulation. In addition, we show that gp130 is constitu tively associated with the cell surface adaptor complex AP-2. Our findings strongly suggest endocytosis of gp130 to be constitutive. (C) 1998 Federati on of European Biochemical Societies.