Fast, Slow, or Not at All The Extracellular Matrix Controls Movement of Signaling Molecules 英文参考文献.docVIP

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Fast, Slow, or Not at All The Extracellular Matrix Controls Movement of Signaling Molecules 英文参考文献.doc

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Fast, Slow, or Not at All The Extracellular Matrix Controls Movement of Signaling Molecules 英文参考文献

Synopsis Fast,Slow,orNotatAll:TheExtracellularMatrixControls MovementofSignalingMolecules RichardRobinson* FreelanceScienceWriter,Sherborn,Massachusetts,UnitedStatesofAmerica Fromelementaryschoolbiologyonup, almosteverydiagramofeverycellincludes asharplinedividinginside—ahiveofwell- ordered biochemical activity—from out- side, usually depicted as a void, with perhaps the occasional signaling molecule drifting randomly and alone toward the plasmamembrane.Butitjustisn’tso.The extracellular matrix is extensive, complex, andvitaltoboththestructureandfunction of the cell. This gelatinous network of sugarsandproteinsnotonlylinksthecellto itsneighbors,itregulatesincomingmolec- ular traffic by binding and transporting a widevarietyofproteins,helpingtocontrol themovementofhormones,cytokines,and growth factors, among others, and estab- lishing gradients of these compounds that are important in the development of the organismandforfightinginfections. Proteoglycansarekeyingredientsofthe matrix, and are the dominant molecule closest to the plasma membrane. Each is composed of a ‘‘core protein’’, some of MontageofafalsecolorphotothermalimageofFGF2-nanoparticlesontwofibroblast cells and of an electron micrograph showing the clustering of FGF2-nanoparticles (blackdots)withasuperimposedtrackofanFGF2(redline). doi:10.1371/journal.pbio.1001362.g001 whichareembeddedinthemembrane,and each is linked to many sugar chains that extendoutward.Oneofthemostcommon and important chains is heparan sulfate (HS),whoserepeatingsugarsanddangling sulfates create multiple binding sites for manydifferentextracellularproteins.Mul- tipleproteinsmaybindtothesamespoton HS with varying affinities, and a single proteinmaybindatseveraldifferentsites. Therichnessofthisarrangementhasmade studying the trafficking of proteins within thematrixachallenge,andlittleisknown aboutthedetailsofthatmovement.Inthis issue of PLoS Biology, Laurence Duchesne, David Fernig, and colleagues use two imagingtechniquestolocatean