Cellular and Molecular Neurobiology

, Volume 30, Issue 5, pp 653–666 | Cite as

Interactions of Prion Protein With Intracellular Proteins: So Many Partners and no Consequences?

Review Paper
First Online:
Received:
Accepted:

Abstract

Prion protein (PrP) plays a key role in the pathogenesis of transmissible spongiform encephalopathies (TSEs)—fatal diseases of the central nervous system. Its physiological function as well as exact role in neurodegeneration remain unclear, hence screens for proteins interacting with PrP seem to be the most promising approach to elucidating these issues. PrP is mostly a plasma membrane-anchored extracellular glycoprotein and only a small fraction resides inside the cell, yet the number of identified intracellular partners of PrP is comparable to that of its membranal or extracellular interactors. Since some TSEs are accompanied by significantly increased levels of cytoplasmic PrP and this fraction of the protein has been found to be neurotoxic, it is of particular interest to characterize the intracellular interactome of PrP. It seems reasonable that at elevated cytoplasmic levels, PrP may exert cytotoxic effect by affecting the physiological functions of its intracellular interactors. This review is focused on the cytoplasmic partners of PrP along with possible consequences of their binding.

Keywords

Prion protein Protein–protein interactions Protein aggregation Transmissible spongiform encephalopathies Neurotoxicity 

Abbreviations

Bcl-2

B-cell lymphoma 2 protein

BSE

Bovine spongiform encephalopathy

C1

N-terminally truncated form of PrP encompassing residues ~110/112–231

C2

N-terminally truncated form of PrP encompassing residues ~90/91–231

CaMKIIα

Calcium/calmodulin-dependent protein kinase α type II

CJD

Creutzfeldt–Jakob disease

CK2

Casein kinase 2

CtmPrP

Transmembrane form of PrP with the C-terminus residing in the lumen of ER

CWD

Chronic wasting disease

cyPrP, cytPrP, cytoPrP

PrP residing entirely in the cytosol

ER

Endoplasmic reticulum

FFI

Fatal familial insomnia

GFAP

Glial fibrillary acidic protein

GPI

Glycosylphosphatidylinositol

Grb2

Growth factor receptor-bound protein 2

GSS

Gerstmann–Sträussler–Scheinker disease

HEK

Human embryonic kidney cells

hnRNP

Heterogeneous nuclear ribonucleoprotein

Hsp

Heat shock protein

MAPs

Microtubule-associated proteins

Mgrn

Mahogunin

NLS

Nuclear localization signal

NRAGE

Neurotrophin receptor-interacting MAGE homolog

Nrf2

Nuclear factor erythroid 2-related factor 2

NtmPrP

Transmembrane form of PrP with the N-terminus residing in the lumen of ER

OR

Octapeptide repeats

PK

Proteinase K

Prnp

Prion protein gene

PrP

Prion protein

PrPC

Cellular form of PrP

PrPSc

Scrapie form of PrP

rPrP

Recombinant PrP

SP

Signal peptide

TM

Transmembrane domain

TSE

Transmissible spongiform encephalopathy

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Notes

Acknowledgments

The author thanks Dr. Hanna Nieznanska for critical reading of the manuscript and helpful comments. This work was supported by a statutory grant to the Nencki Institute of Experimental Biology from the Ministry of Science and Higher Education.

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© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Department of Biochemistry, Polish Academy of SciencesNencki Institute of Experimental BiologyWarsawPoland

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