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. 2017 Apr 6;4:19. doi: 10.3389/fmolb.2017.00019

Table 2.

Reported interacting partners of PrPC.

Protein/protein complex Subcellular localisation and function Method References
14-3-3 protein Cytoplasmic adaptor protein involved in multiple signalling pathways Interactomics; co-IP Satoh et al., 2005; Zafar et al., 2011
37/67 kDa laminin receptor Cell surface receptor for laminin (see below) Binding assay; yeast two-hybrid; co-IP Gauczynski et al., 2001; Hundt et al., 2001
60 kDa heat shock protein Mitochondrial chaperone Interactomics; co-IP Satoh et al., 2005; Zafar et al., 2011
Annexin A2 Calcium-regulated cell membrane protein with a poorly defined function Interactomics; co-IP Morel et al., 2008; Zafar et al., 2011
Desmoplakin Organisation of cell junctions Interactomics; co-IP Morel et al., 2008; Besnier et al., 2015
Dipeptidyl aminopeptidase-like protein 6 Cell membrane protein that binds to and modulates activity of potassium channels Interactomics; co-IP Schmitt-Ulms et al., 2004; Mercer et al., 2013
Doppel Cell membrane protein of unknown function Co-IP Qin et al., 2006; Caputo et al., 2010
Junction plakoglobin (a.k.a. γ-catenin) Organisation of cell junctions Interactomics; yeast two-hybrid Besnier et al., 2015; Lappas Gimenez et al., 2015
Laminin Extracellular matrix protein with multiple functions (cell migration, adhesion, differentiation…) Binding assay Graner et al., 2000a; Coitinho et al., 2006
Lactate dehydrogenase Cytoplasmic enzyme that converts lactate to pyruvate and vice versa Interactomics; co-IP Zafar et al., 2011; Ramljak et al., 2015
Metabotropic glutamate receptor Cell surface receptor for the neurotransmitter glutamate Co-IP; binding assay Beraldo et al., 2011; Haas et al., 2014
Neural cell adhesion molecule 1 Cell membrane protein with multiple functions (adhesion, neurite outgrowth…) Co-IP; binding assay Schmitt-Ulms et al., 2001; Santuccione et al., 2005
Nicotinic acetylcholine receptor Cell surface receptor for the neurotransmitter acetylcholine Co-IP; binding assay Petrakis et al., 2008; Beraldo et al., 2010
Stress-induced phosphoprotein 1 Cytoplasmic co-chaperone; may also be secreted to function as a PrPC ligand Binding assay; co-IP Zanata et al., 2002; Lopes et al., 2005
Tubulin Cytoskeletal protein (microtubules) Interactomics; co-IP Nieznanski et al., 2005; Zafar et al., 2011
Vimentin Cytoskeletal protein (intermediate filaments) Interactomics; yeast two-hybrid Zafar et al., 2011; Lappas Gimenez et al., 2015

Some of the proteins that may interact with PrPC. Numerous interacting partners have been suggested but we include only those proteins for which two separate references could be found that provided direct evidence of an interaction with PrPC. This is not meant to indicate that interactions identified in a single reference are incorrect, especially in the case of recently identified interactions. It is also important to state that certain techniques, such as co-immunoprecipitation (co-IP), do not distinguish between indirect and direct interactions. Therefore, some of the proteins listed in this table may interact with PrPC indirectly.