CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain
Ostuni M, Guellec J, Hermand P, Durand P, Combadière C, Pincet F, Deterre P. CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain. Biology Open 2014, 3: 1173-1182. PMID: 25395671, PMCID: PMC4265755, DOI: 10.1242/bio.20149845.Peer-Reviewed Original ResearchCytosolic domainTransmembrane domainChemokine domainMucin stalkMembrane domainsHigh glycosylationFunctional rolePatrolling behaviorFunctional adhesion assaysAdhesion assaysCritical roleGlycosylationDomainCytoskeletonPermanent aggregationStructural analysisStalkAdhesionRoleMembraneCX3CL1CellsAssaysReceptorsCalcium sensitive ring-like oligomers formed by synaptotagmin
Wang J, Bello O, Auclair SM, Wang J, Coleman J, Pincet F, Krishnakumar SS, Sindelar CV, Rothman JE. Calcium sensitive ring-like oligomers formed by synaptotagmin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 13966-13971. PMID: 25201968, PMCID: PMC4183308, DOI: 10.1073/pnas.1415849111.Peer-Reviewed Original ResearchConceptsSynaptic vesicle protein Synaptotagmin 1Cytosolic domainSoluble N-ethylmaleimide-sensitive factorN-ethylmaleimide-sensitive factorMembrane fusion machineryReceptor complex assemblyRing-like oligomersFusion machineryC2 domainComplex assemblySynaptotagmin-1Helical reconstructionFusion proceedsNovel mechanismStructural mechanismsLipid monolayersNeurotransmitter releaseAbsence of calciumPhysiological concentrationsRing formationPresence of calciumFree calcium ionsSynaptotagminCalcium influxCircular arrangement