CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain

Mariano Ostuni 1 Julie Guellec 1 Patricia Hermand 1 Pauline Durand 2 Christophe Combadière 1 Frédéric Pincet 2 Philippe Deterre 1, *
* Auteur correspondant
1 CIMI - Centre d'Immunologie et de Maladies Infectieuses
2 LPS - Laboratoire de Physique Statistique de l'ENS
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.
Keywords : Chemokine Adhesion FRAP Glycosylation GPCR
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Article dans une revue
Biology Open, Royal Society, 2014, 3, pp.1173-1182. 〈10.1242/bio.20149845〉
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Mariano Ostuni, Julie Guellec, Patricia Hermand, Pauline Durand, Christophe Combadière, et al.. CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain. Biology Open, Royal Society, 2014, 3, pp.1173-1182. 〈10.1242/bio.20149845〉. 〈inserm-01095507〉

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