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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1915

Uelhoff, A; Tatzelt, J; Aguzzi, A; Winklhofer, K F; Haass, C (2005). A pathogenic PrP mutation and doppel interfere with polarized sorting of the prion protein. Journal of Biological Chemistry, 280(7):5137-5140.

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Abstract

Several proteins linked to neurodegenerative diseases, such as the beta-amyloid precursor protein, amyloid beta-peptide, beta-secretase, and tau, undergo selective polarized sorting. We investigated polarized sorting of the mammalian prion protein (PrP(C)) and its homologue doppel (Dpl). In contrast to Dpl, which accumulates on the apical surface, PrP(C) is targeted selectively to the basolateral side in Madin-Darby canine kidney cells. An extensive deletion and domain swapping analysis revealed that the internal hydrophobic domain (HD) of PrP (amino acids 113-133) confers basolateral sorting in a dominant manner. PrP mutants lacking the HD are sorted apically, while Dpl chimeras containing the HD of PrP are directed to the basolateral membrane. Furthermore, a pathogenic PrP missense mutation within the HD leads to aberrant apical sorting of PrP as well.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:18 February 2005
Deposited On:11 Feb 2008 13:26
Last Modified:28 Nov 2013 02:23
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Publisher DOI:10.1074/jbc.C400560200
PubMed ID:15615717
Citations:Web of Science®. Times Cited: 30
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