Cargando…
Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane
Munc18-1 plays pleiotropic roles in neurosecretion by acting as 1) a molecular chaperone of syntaxin-1, 2) a mediator of dense-core vesicle docking, and 3) a priming factor for soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion. However, how these function...
Autores principales: | Han, Gayoung A., Malintan, Nancy T., Saw, Ner Mu Nar, Li, Lijun, Han, Liping, Meunier, Frederic A., Collins, Brett M., Sugita, Shuzo |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3204074/ https://www.ncbi.nlm.nih.gov/pubmed/21900502 http://dx.doi.org/10.1091/mbc.E11-02-0135 |
Ejemplares similares
-
Synaptic Vesicle Docking: Sphingosine Regulates Syntaxin1 Interaction with Munc18
por: Camoletto, Paola G., et al.
Publicado: (2009) -
Vacuolar H(+)-ATPase subunits Voa1 and Voa2 cooperatively regulate secretory vesicle acidification, transmitter uptake, and storage
por: Saw, Ner Mu Nar, et al.
Publicado: (2011) -
Syntaxins on granules promote docking of granules via interactions with munc18
por: Borisovska, Maria
Publicado: (2018) -
The Munc18-1 domain 3a hinge-loop controls syntaxin-1A nanodomain assembly and engagement with the SNARE complex during secretory vesicle priming
por: Kasula, Ravikiran, et al.
Publicado: (2016) -
A Flexible Syntaxin Solves the Mystery of the SNAREd Munc
por: Robinson, Richard
Publicado: (2006)