title: A common exocytotic mechanism mediates axonal and dendritic outgrowth.
abstract: Outgrowth of the dendrites and the axon is the basis of the establishment of the neuronal shape, and it requires addition of new membrane to both growing processes. It is not yet clear whether one or two exocytotic pathways are responsible for the respective outgrowth of axons and dendrites. We have previously shown that tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) defines a novel network of tubulovesicular structures present both at the leading edge of elongating dendrites and axons of immature hippocampal neurons developing in primary culture and that TI-VAMP is an essential protein for neurite outgrowth in PC12 cells. Here we show that the expression of the N-terminal domain of TI-VAMP inhibits the outgrowth of both dendrites and axons in neurons in primary culture. This effect is more prominent at the earliest stages of the development of neurons in vitro. Expression of the N-terminal domain deleted form of TI-VAMP has the opposite effect. This constitutively active form of TI-VAMP localizes as the endogenous protein, particularly concentrating at the leading edge of growing axons. Our results suggest that a common exocytotic mechanism that relies on TI-VAMP mediates both axonal and dendritic outgrowth in developing neurons.
authors.affiliation: Membrane Traffic and Neuronal Plasticity, Institut National de la Santé et de la Recherche Médicale U536, Institut du Fer-à-Moulin, F-75005 Paris, France.
authors.forename: S
authors.initials: S
authors.lastname: Martinez-Arca
authors.forename: S
authors.initials: S
authors.lastname: Coco
authors.forename: G
authors.initials: G
authors.lastname: Mainguy
authors.forename: U
authors.initials: U
authors.lastname: Schenk
authors.forename: P
authors.initials: P
authors.lastname: Alberts
authors.forename: P
authors.initials: P
authors.lastname: Bouillé
authors.forename: M
authors.initials: M
authors.lastname: Mezzina
authors.forename: A
authors.initials: A
authors.lastname: Prochiantz
authors.forename: M
authors.initials: M
authors.lastname: Matteoli
authors.forename: D
authors.initials: D
authors.lastname: Louvard
authors.forename: T
authors.initials: T
authors.lastname: Galli
mesh_terms: D000818:Animals; D001324:Autoantigens; D001369:Axons / Q000502:physiology*; D001921:Brain / Q000166:cytology / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D037282:Calreticulin; D002478:Cells, Cultured; D003712:Dendrites / Q000502:physiology*; D018274:Electroporation; D004705:Endocytosis / Q000502:physiology; D005089:Exocytosis / Q000502:physiology*; D015870:Gene Expression; D049452:Green Fluorescent Proteins; D066298:In Vitro Techniques; D008164:Luminescent Proteins / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D051379:Mice; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism; D014162:Transfection
chemical_list: D001324:Autoantigens; D002135:Calcium-Binding Proteins; D037282:Calreticulin; C097741:Golgin subfamily A member 2; D008164:Luminescent Proteins; D008565:Membrane Proteins; D020033:Protein Isoforms; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D011993:Recombinant Fusion Proteins; D012261:Ribonucleoproteins; D049452:Green Fluorescent Proteins