Spatial and proteomic profiling reveals ...
Type de document :
Article dans une revue scientifique: Article original
DOI :
PMID :
URL permanente :
Titre :
Spatial and proteomic profiling reveals centrosome-independent features of centriolar satellites
Auteur(s) :
Gheiratmand, Ladan [Auteur]
Coyaud, Etienne-Marie [Auteur]
Gupta, Gagan D. [Auteur]
Laurent, Estelle [Auteur]
Hasegan, Monica [Auteur]
Prosser, Suzanna L. [Auteur]
Goncalves, Joao [Auteur]
Raught, Brian [Auteur]
Pelletier, Laurence [Auteur]
Coyaud, Etienne-Marie [Auteur]
Gupta, Gagan D. [Auteur]
Laurent, Estelle [Auteur]
Hasegan, Monica [Auteur]
Prosser, Suzanna L. [Auteur]
Goncalves, Joao [Auteur]
Raught, Brian [Auteur]
Pelletier, Laurence [Auteur]
Titre de la revue :
The EMBO Journal
Nom court de la revue :
Embo J.
Numéro :
38
Pagination :
-
Date de publication :
2019-07-15
ISSN :
0261-4189
Mot(s)-clé(s) :
centrinone
centriolar satellites
proteomics
centrosome
BioID
centriolar satellites
proteomics
centrosome
BioID
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
Centriolar satellites are small electron-dense granules that cluster in the vicinity of centrosomes. Satellites have been implicated in multiple critical cellular functions including centriole duplication, centrosome ...
Lire la suite >Centriolar satellites are small electron-dense granules that cluster in the vicinity of centrosomes. Satellites have been implicated in multiple critical cellular functions including centriole duplication, centrosome maturation, and ciliogenesis, but their precise composition and assembly properties have remained poorly explored. Here, we perform in vivo proximity-dependent biotin identification (BioID) on 22 human satellite proteins, to identify 2,113 high-confidence interactions among 660 unique polypeptides. Mining this network, we validate six additional satellite components. Analysis of the satellite interactome, combined with subdiffraction imaging, reveals the existence of multiple unique microscopically resolvable satellite populations that display distinct protein interaction profiles. We further show that loss of satellites in PCM1-depleted cells results in a dramatic change in the satellite interaction landscape. Finally, we demonstrate that satellite composition is largely unaffected by centriole depletion or disruption of microtubules, indicating that satellite assembly is centrosome-independent. Together, our work offers the first systematic spatial and proteomic profiling of human centriolar satellites and paves the way for future studies aimed at better understanding the biogenesis and function(s) of these enigmatic structures.Lire moins >
Lire la suite >Centriolar satellites are small electron-dense granules that cluster in the vicinity of centrosomes. Satellites have been implicated in multiple critical cellular functions including centriole duplication, centrosome maturation, and ciliogenesis, but their precise composition and assembly properties have remained poorly explored. Here, we perform in vivo proximity-dependent biotin identification (BioID) on 22 human satellite proteins, to identify 2,113 high-confidence interactions among 660 unique polypeptides. Mining this network, we validate six additional satellite components. Analysis of the satellite interactome, combined with subdiffraction imaging, reveals the existence of multiple unique microscopically resolvable satellite populations that display distinct protein interaction profiles. We further show that loss of satellites in PCM1-depleted cells results in a dramatic change in the satellite interaction landscape. Finally, we demonstrate that satellite composition is largely unaffected by centriole depletion or disruption of microtubules, indicating that satellite assembly is centrosome-independent. Together, our work offers the first systematic spatial and proteomic profiling of human centriolar satellites and paves the way for future studies aimed at better understanding the biogenesis and function(s) of these enigmatic structures.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
INSERM
Université de Lille
Université de Lille
Date de dépôt :
2022-06-15T13:59:05Z