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Status: Bibliographieeintrag

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Verfasst von:Glomb, Oliver [VerfasserIn]   i
 Wu, Yehui [VerfasserIn]   i
 Rieger, Lucia [VerfasserIn]   i
 Rüthnick, Diana [VerfasserIn]   i
Titel:The cell polarity proteins Boi1 and Boi2 direct an actin nucleation complex to sites of exocytosis in Saccharomyces cerevisiae
Verf.angabe:Oliver Glomb, Yehui Wu, Lucia Rieger, Diana Ruethnick, Medhanie A. Mulaw and Nils Johnsson
Jahr:2020
Jahr des Originals:2019
Umfang:15 S.
Fussnoten:Accepted 19 December 2019 ; Gesehen am 07.04.2020
Titel Quelle:Enthalten in: Journal of cell science
Ort Quelle:Cambridge : Company of Biologists Limited, 1853
Jahr Quelle:2020
Band/Heft Quelle:133(2020), 3, Seite jcs237982
ISSN Quelle:1477-9137
Abstract:Owing to the local enrichment of factors that influence its dynamics and organization, the actin cytoskeleton displays different shapes and functions within the same cell. In yeast cells, post-Golgi vesicles ride on long actin cables to the bud tip. The proteins Boi1 and Boi2 (Boi1/2) participate in tethering and docking these vesicles to the plasma membrane. Here, we show in Saccharomyces cerevisiae that Boi1/2 also recruit nucleation and elongation factors to form actin filaments at sites of exocytosis. Disrupting the connection between Boi1/2 and the nucleation factor Bud6 impairs filament formation, reduces the directed movement of the vesicles to the tip and shortens the vesicles' tethering time at the cortex. Transplanting Boil from the bud tip to the peroxisomal membrane partially redirects the actin cytoskeleton and the vesicular flow towards the peroxisome, and creates an alternative, rudimentary vesicle-docking zone. We conclude that Boi1/2, through interactions with Bud6 and Bni1, induce the formation of a cortical actin structure that receives and aligns incoming vesicles before fusion with the membrane.
DOI:doi:10.1242/jcs.237982
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.

Volltext: https://doi.org/10.1242/jcs.237982
 DOI: https://doi.org/10.1242/jcs.237982
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Actin nucleation
 cdc42
 Cdc42
 exocyst complex
 formin
 interacts
 myosin-v
 plasma-membrane
 Polar growth
 promotes
 reveals
 secretory vesicles
 split-ubiquitin
 Split-Ubiquitin
 Vesicular traffic
 Yeast
K10plus-PPN:1694175022
Verknüpfungen:→ Zeitschrift

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