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Status: Bibliographieeintrag

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Verfasst von:Kumar, Rajesh [VerfasserIn]   i
 Neuser, Nicole [VerfasserIn]   i
 Tyedmers, Jens [VerfasserIn]   i
Titel:Hitchhiking vesicular transport routes to the vacuole
Titelzusatz:amyloid recruitment to the Insoluble Protein Deposit (IPOD)
Verf.angabe:Rajesh Kumar, Nicole Neuser, and Jens Tyedmers
E-Jahr:2017
Jahr:22 Mar 2017
Umfang:11 S.
Fussnoten:Gesehen am 09.11.2018
Titel Quelle:Enthalten in: Prion
Ort Quelle:London [u.a.] : Taylor & Francis, 2007
Jahr Quelle:2017
Band/Heft Quelle:11(2017), 2, Seite 71-81
ISSN Quelle:1933-690X
Abstract:Sequestration of aggregates into specialized deposition sites occurs in many species across all kingdoms of life ranging from bacteria to mammals and is commonly believed to have a cytoprotective function. Yeast cells possess at least 3 different spatially separated deposition sites, one of which is termed “Insoluble Protein Deposit (IPOD)” and harbors amyloid aggregates. We have recently discovered that recruitment of amyloid aggregates to the IPOD uses an actin cable based recruitment machinery that also involves vesicular transport.1 Here we discuss how different proteins known to be involved in vesicular transport processes to the vacuole might act to guide amyloid aggregates to the IPOD. These factors include the Myosin V motor protein Myo2 involved in transporting vacuolar vesicles along actin cables, the transmembrane protein Atg9 involved in the recruitment of large precursor hydrolase complexes to the vacuole, the phosphatidylinositol/ phosphatidylcholine (PI/PC) transfer protein Sec 14 and the SNARE chaperone Sec 18. Furthermore, we present new data suggesting that the yeast dynamin homolog Vps1 is also crucial for faithful delivery of the amyloid model protein PrD-GFP to the IPOD. This is in agreement with a previously identified role for Vps1 in recruitment of heat-denatured aggregates to a perivacuolar deposition site.
DOI:doi:10.1080/19336896.2017.1293226
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 ; Verlag: http://dx.doi.org/10.1080/19336896.2017.1293226
 kostenfrei: Volltext: https://doi.org/10.1080/19336896.2017.1293226
 DOI: https://doi.org/10.1080/19336896.2017.1293226
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:actin
 amyloid aggregates
 Atg9 vesicles
 Cytoplasm-to-vacuole targeting (CVT) pathway
 Insoluble Protein Deposit (IPOD)
 Myosin motor protein Myo2
 Phagophore Assembly Site (PAS)
 prions
 Sec 14
 Sec 18
 vesicular transport
 Vps1
 yeast (Saccharomyces cerevisiae)
K10plus-PPN:1582749892
Verknüpfungen:→ Zeitschrift

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