Stochastic palmitoylation of accessible cysteines in membrane proteins revealed by native mass spectrometry
Cysteine palmitoylation affects the localization and function of membrane proteins, but its stoichiometry and specificity are not well understood. Here, the authors show that palmitoylation is a stochastic process that depends on the accessibility of cysteines rather than a defined substrate motif.
Guardado en:
Autores principales: | Remco N. P. Rodenburg, Joost Snijder, Michiel van de Waterbeemd, Arie Schouten, Joke Granneman, Albert J. R. Heck, Piet Gros |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/31d2d794c1834117b8a67cef2fedf804 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
por: Wout Oosterheert, et al.
Publicado: (2018) -
A cluster of palmitoylated cysteines are essential for aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis
por: Cinta Diez-Ardanuy, et al.
Publicado: (2017) -
Adeno-associated virus capsid assembly is divergent and stochastic
por: Tobias P. Wörner, et al.
Publicado: (2021) -
Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods
por: Michiel van de Waterbeemd, et al.
Publicado: (2018) -
Protein Palmitoylation in Bovine Ovarian Follicle
por: Svetlana Uzbekova, et al.
Publicado: (2021)