Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.

cellular prion protein gene mutations prion diseases protein–protein interactions signal transduction

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
25 Sep 2020
Historique:
received: 31 07 2020
revised: 20 09 2020
accepted: 23 09 2020
entrez: 30 9 2020
pubmed: 1 10 2020
medline: 3 3 2021
Statut: epublish

Résumé

Cellular prion protein (PrPc) is a small glycosylphosphatidylinositol (GPI) anchored protein most abundantly found in the outer leaflet of the plasma membrane (PM) in the central nervous system (CNS). PrPc misfolding causes neurodegenerative prion diseases in the CNS. PrPc interacts with a wide range of protein partners because of the intrinsically disordered nature of the protein's N-terminus. Numerous studies have attempted to decipher the physiological role of the prion protein by searching for proteins which interact with PrPc. Biochemical characteristics and biological functions both appear to be affected by interacting protein partners. The key challenge in identifying a potential interacting partner is to demonstrate that binding to a specific ligand is necessary for cellular physiological function or malfunction. In this review, we have summarized the intracellular and extracellular interacting partners of PrPc and potential consequences of their binding. We also briefly describe prion disease-related mutations at the end of this review.

Identifiants

pubmed: 32992764
pii: ijms21197058
doi: 10.3390/ijms21197058
pmc: PMC7583789
pii:
doi:

Substances chimiques

Ligands 0
Prion Proteins 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Natural Sciences and Engineering Research Council of Canada
ID : 414612

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Auteurs

Hajar Miranzadeh Mahabadi (H)

Department of Anatomy, Physiology, Pharmacology, College of Medicine, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada.

Changiz Taghibiglou (C)

Department of Anatomy, Physiology, Pharmacology, College of Medicine, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada.

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