Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Aslanyan, Mariam [VerfasserIn]   i
 Doornbos, Cenna [VerfasserIn]   i
 Diwan, Gaurav [VerfasserIn]   i
 Anvarian, Zeinab [VerfasserIn]   i
 Beyer, Tina [VerfasserIn]   i
 Junger, Katrin [VerfasserIn]   i
 van Beersum, Sylvia E.C. [VerfasserIn]   i
 Russell, Robert B. [VerfasserIn]   i
 Ueffing, Marius [VerfasserIn]   i
 Ludwig, Alexander [VerfasserIn]   i
 Boldt, Karsten [VerfasserIn]   i
 Pedersen, Lotte B. [VerfasserIn]   i
 Roepman, Ronald [VerfasserIn]   i
Titel:A targeted multi-proteomics approach generates a blueprint of the ciliary ubiquitinome
Verf.angabe:Mariam G. Aslanyan, Cenna Doornbos, Gaurav D. Diwan, Zeinab Anvarian, Tina Beyer, Katrin Junger, Sylvia E.C. van Beersum, Robert B. Russell, Marius Ueffing, Alexander Ludwig, Karsten Boldt, Lotte B. Pedersen and Ronald Roepman
E-Jahr:2023
Jahr:26 January 2023
Umfang:19 S.
Fussnoten:Gesehen am 12.04.2023
Titel Quelle:Enthalten in: Frontiers in cell and developmental biology
Ort Quelle:Lausanne : Frontiers Media, 2013
Jahr Quelle:2023
Band/Heft Quelle:11(2023), Artikel-ID 1113656, Seite 1-19
ISSN Quelle:2296-634X
Abstract:Establishment and maintenance of the primary cilium as a signaling-competent organelle requires a high degree of fine tuning, which is at least in part achieved by a variety of post-translational modifications. One such modification is ubiquitination. The small and highly conserved ubiquitin protein possesses a unique versatility in regulating protein function via its ability to build mono and polyubiquitin chains onto target proteins. We aimed to take an unbiased approach to generate a comprehensive blueprint of the ciliary ubiquitinome by deploying a multi-proteomics approach using both ciliary-targeted ubiquitin affinity proteomics, as well as ubiquitin-binding domain-based proximity labelling in two different mammalian cell lines. This resulted in the identification of several key proteins involved in signaling, cytoskeletal remodeling and membrane and protein trafficking. Interestingly, using two different approaches in IMCD3 and RPE1 cells, respectively, we uncovered several novel mechanisms that regulate cilia function. In our IMCD3 proximity labeling cell line model, we found a highly enriched group of ESCRT-dependent clathrin-mediated endocytosis-related proteins, suggesting an important and novel role for this pathway in the regulation of ciliary homeostasis and function. In contrast, in RPE1 cells we found that several structural components of caveolae (CAV1, CAVIN1, and EHD2) were highly enriched in our cilia affinity proteomics screen. Consistently, the presence of caveolae at the ciliary pocket and ubiquitination of CAV1 specifically, were found likely to play a role in the regulation of ciliary length in these cells. Cilia length measurements demonstrated increased ciliary length in RPE1 cells stably expressing a ubiquitination impaired CAV1 mutant protein. Furthermore, live cell imaging in the same cells revealed decreased CAV1 protein turnover at the cilium as the possible cause for this phenotype. In conclusion, we have generated a comprehensive list of cilia-specific proteins that are subject to regulation via ubiquitination which can serve to further our understanding of cilia biology in health and disease.
DOI:doi:10.3389/fcell.2023.1113656
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

kostenfrei: Volltext: https://doi.org/10.3389/fcell.2023.1113656
 kostenfrei: Volltext: https://www.frontiersin.org/articles/10.3389/fcell.2023.1113656/full
 DOI: https://doi.org/10.3389/fcell.2023.1113656
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:caveolae
 cilia
 cilia ubiquitination
 ciliary proteostasis
 ciliogenesis
 ciliopathies
 clathrin-mediated endocytosis
 components
 escrt
 genes
 identification
 ligase
 membrane
 proteins
 reveals
 trafficking
K10plus-PPN:1842084550
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/69064744   QR-Code
zum Seitenanfang