mmpc-logo mmpc-logo
twitter-logo    bluesky-logo
| Create Account | login
Publication
Implications of the differing roles of the ß1 and ß3 transmembrane and
cytoplasmic domains for integrin function.
Authors Lu Z, Mathew S, Chen J, Hadziselimovic A, Palamuttam R, Hudson BG, Fässler R,
Pozzi A, Sanders CR, Zent R
Submitted By Submitted Externally on 1/9/2017
Status Published
Journal eLife
Year 2016
Date Published 12/1/2016
Volume : Pages 5 : Not Specified
PubMed Reference 27929375
Abstract Integrins are transmembrane receptors composed of a and ß subunits. Although
most integrins contain ß1, canonical activation mechanisms are based on studies
of the platelet integrin, aIIbß3. Its inactive conformation is characterized by
the association of the aIIb transmembrane and cytosolic domain (TM/CT) with a
tilted ß3 TM/CT that leads to activation when disrupted. We show significant
structural differences between ß1 and ß3 TM/CT in bicelles. Moreover, the
'snorkeling' lysine at the TM/CT interface of ß subunits, previously proposed to
regulate aIIbß3 activation by ion pairing with nearby lipids, plays opposite
roles in ß1 and ß3 integrin function and in neither case is responsible for TM
tilt. A range of affinities from almost no interaction to the relatively high
avidity that characterizes aIIbß3 is seen between various a subunits and ß1
TM/CTs. The aIIbß3-based canonical model for the roles of the TM/CT in integrin
activation and function clearly does not extend to all mammalian integrins.




Menu

Home
Contact
About MMPC
Animal Husbandry
Tests Data
Search Data
Analysis
Clients
MMPC Centers

Newsletter

Interested in receiving MMPC News?
twitter-logo Mouse Phenotyping
@NationalMMPC



2017 National MMPC. All Rights Reserved.