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Titel: The signal peptide plus a cluster of positive charges in prion protein dictate chaperone-mediated Sec61 channel gating
VerfasserIn: Ziska, Anke
Tatzelt, Jörg
Dudek, Johanna
Paton, Adrienne W.
Paton, James C.
Zimmermann, Richard
Haßdenteufel, Sarah
Sprache: Englisch
Titel: Biology open
Bandnummer: 8
Heft: 3
Verlag/Plattform: Company
Erscheinungsjahr: 2019
DDC-Sachgruppe: 610 Medizin, Gesundheit
Dokumenttyp: Journalartikel / Zeitschriftenartikel
Abstract: The Sec61-complex as a dynamic polypeptide-conducting channel mediates protein transport into the human endoplasmic reticulum (ER) with the help of additional components. ER membrane resident Hsp40-type co-chaperone Sec63 as well as the ER lumenal Hsp70-type chaperone BiP were proposed to facilitate channel opening in a precursor-specific fashion. Here, we report on their rules of engagement in ER import of the prion protein (PrP) by addressing sixteen PrP-related variants which differ in their signal peptides and mature parts, respectively. Transport into the ER of semi-permeabilized human cells was analyzed upon depletion of the components by siRNA- or toxin-treatment. The results are consistent with the view of separate functions of BiP and Sec63 and strongly suggest that the co-chaperone/chaperone-pair facilitates Sec61 channel gating to the open state when precursor polypeptides with weak signal peptides in combination with detrimental features in the adjacent mature part were targeted. Thus, we expand the view of chaperone-mediated Sec61 channel gating by providing a novel example of a polybasic motif that interferes with signal peptide-mediated Sec61 channel gating. This article has an associated First Person interview with the first author of the paper.
DOI der Erstveröffentlichung: 10.1242/bio.040691
URL der Erstveröffentlichung: https://journals.biologists.com/bio/article/8/3/bio040691/1774/The-signal-peptide-plus-a-cluster-of-positive
Link zu diesem Datensatz: urn:nbn:de:bsz:291--ds-442957
hdl:20.500.11880/39585
http://dx.doi.org/10.22028/D291-44295
ISSN: 2046-6390
Datum des Eintrags: 5-Feb-2025
Fakultät: M - Medizinische Fakultät
Fachrichtung: M - Medizinische Biochemie und Molekularbiologie
Professur: M - Keiner Professur zugeordnet
Sammlung:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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