Abstract:
:The transmembrane protein gp130 is the common signalling receptor subunit for 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 studied 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 independent from IL-6/IL-6R stimulation. In addition, we show that gp130 is constitutively associated with the cell surface adaptor complex AP-2. Our findings strongly suggest endocytosis of gp130 to be constitutive.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Thiel S,Dahmen H,Martens A,Müller-Newen G,Schaper F,Heinrich PC,Graeve Ldoi
10.1016/s0014-5793(98)01559-2subject
Has Abstractpub_date
1998-12-18 00:00:00pages
231-4issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01559-2journal_volume
441pub_type
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