Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Miller, Stephanie Barbara Maria [VerfasserIn]   i
 Mogk, Axel [VerfasserIn]   i
 Bukau, Bernd [VerfasserIn]   i
Titel:Spatially Organized Aggregation of Misfolded Proteins as Cellular Stress Defense Strategy
Verf.angabe:Stephanie B. M. Miller, Axel Mogk and Bernd Bukau
E-Jahr:2015
Jahr:11 February 2015
Umfang:11 S.
Fussnoten:Gesehen am 08.06.2020
Titel Quelle:Enthalten in: Journal of molecular biology
Ort Quelle:Amsterdam [u.a.] : Elsevier, 1959
Jahr Quelle:2015
Band/Heft Quelle:427(2015), 7, Seite 1564-1574
ISSN Quelle:1089-8638
Abstract:An evolutionary conserved response of cells to proteotoxic stress is the organized sequestration of misfolded proteins into subcellular deposition sites. In Saccharomyces cerevisiae, three major sequestration sites for misfolded proteins exist, IPOD (insoluble protein deposit), INQ (intranuclear quality control compartment) [former JUNQ (juxtanuclear quality control compartment)] and CytoQ. IPOD is perivacuolar and predominantly sequesters amyloidogenic proteins. INQ and CytoQs are stress-induced deposits for misfolded proteins residing in the nucleus and the cytosol, respectively, and requiring cell-compartment-specific aggregases, nuclear Btn2 and cytosolic Hsp42 for formation. The organized aggregation of misfolded proteins is proposed to serve several purposes collectively increasing cellular fitness and survival under proteotoxic stress. These include (i) shielding of cellular processes from interference by toxic protein conformers, (ii) reducing the substrate burden for protein quality control systems upon immediate stress, (iii) orchestrating chaperone and protease functions for efficient repair or degradation of damaged proteins [this involves initial extraction of aggregated molecules via the Hsp70/Hsp104 bi-chaperone system followed by either refolding or proteasomal degradation or removal of entire aggregates by selective autophagy (aggrephagy) involving the adaptor protein Cue5] and (iv) enabling asymmetric retention of protein aggregates during cell division, thereby allowing for damage clearance in daughter cells. Regulated protein aggregation thus serves cytoprotective functions vital for the maintenance of cell integrity and survival even under adverse stress conditions and during aging.
DOI:doi:10.1016/j.jmb.2015.02.006
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 ; Verlag: https://doi.org/10.1016/j.jmb.2015.02.006
 Volltext: http://www.sciencedirect.com/science/article/pii/S002228361500100X
 DOI: https://doi.org/10.1016/j.jmb.2015.02.006
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:autophagy
 chaperone
 heat shock proteins
 proteasome
 protein aggregation
K10plus-PPN:1700132792
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68585141   QR-Code
zum Seitenanfang