 |
Journal articles
CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain
Abstract : The multi-domain CX3CL1 transmembrane chemokine triggers leukocyte adherence without rolling and migration by presentingits chemokine domain (CD) to its receptor CX3CR1. Through the combination of functional adhesion assays with structural analysis using FRAP, we investigated the functional role of the other domains of CX3CL1, i.e., its mucin stalk, transmembrane domain and cytosolic domain. Our results indicate that the CX3CL1 molecular structure is finely adapted to capture CX3CR1 incirculating cells and that each domain has a specific purpose: the mucin stalk is stiffened by its high glycosylation to present the CD away from the membrane, the transmembrane domain generates the permanent aggregation of an adequate amount of monomers to guarantee adhesion and prevent rolling, and the cytosolic domain ensures adhesive robustness by interacting with the cytoskeleton. We propose a model in which quasi-immobile CX3CL1 bundles are organized to quickly generate adhesive patches with sufficiently high strength to capture CX3CR1+ leukocytes but with sufficiently low strength to allow their patrolling behavior.
Cited literature [60 references]
https://www.hal.inserm.fr/inserm-01095507
Contributor : Philippe Deterre <>
Submitted on : Monday, December 15, 2014 - 4:51:20 PM
Last modification on : Monday, November 9, 2020 - 6:16:04 PM
Long-term archiving on: : Saturday, April 15, 2017 - 8:37:34 AM
Contributor : Philippe Deterre <>
Submitted on : Monday, December 15, 2014 - 4:51:20 PM
Last modification on : Monday, November 9, 2020 - 6:16:04 PM
Long-term archiving on: : Saturday, April 15, 2017 - 8:37:34 AM
File
Ostuni_BiologyOpen-2014.pdf
Publisher files allowed on an open archive