Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80.

Abstract:

:Interleukin (IL)-6 is an important cytokine in inflammatory processes, differentiation and growth. The IL-6 receptor complex comprises the specific IL-6 receptor (gp80) and two molecules of the signal tranducing component gp130 which transduces the signal into the nucleus via the Jak-STAT pathway. Both, gp80 and gp130 are sorted preferentially to the basolateral membrane of polarised Madin-Darby canine kidney (MDCK) cells. Previously, we have shown that gp130 partially localises to detergent-resistant membranes (DRMs)/lipid rafts and that lipid raft integrity is crucial for signalling to occur. Here we now demonstrate that wild-type gp80 is associated with DRMs only to a minor extent. However, gp80 mutants which lack parts of the cytoplasmic domain and therefore are more apically expressed than the wild type show an increased affinity for the liquid-ordered membrane domain. Studies with non-polarised MDCK cells suggest that the lipid raft association of the different mutants of gp80 precedes the establishment of cell polarity. Our findings suggest that lipid rafts play a role in the sorting of apically targeted gp80.

journal_name

Eur J Cell Biol

authors

Buk DM,Renner O,Graeve L

doi

10.1016/j.ejcb.2005.06.001

subject

Has Abstract

pub_date

2005-10-01 00:00:00

pages

819-31

issue

10

eissn

0171-9335

issn

1618-1298

pii

S0171-9335(05)00100-7

journal_volume

84

pub_type

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