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Statements

PRNP binds CANX. 11 / 15
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"Interaction of Prion Protein and Shadoo with the ER Chaperon Calnexin in the Lipid-Raft and Non-Raft Membrane Domains."
34940479
sparser
"Therefore, we were intrigued to examine whether this interaction of PrP and CNX is confined to raft- or non-raft-type membranes, and we wanted to test whether CNX is also a binding partner of Sho."
34940479
sparser
"For PrP, the Ni-NTA-bead pull-down experiments on the total lysates of PrP-EGFP cells confirm the presence of CNX in the bead-pulled PrP-containing eluates ( xref A), confirming that CNX may bind PrP, in line with earlier observations by Wang and coworkers [ xref ]."
34940479
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"Next, we aimed to analyze if there is any preference for the interaction of prion proteins and calnexin depending on the type of membrane domains that the proteins reside in."
34940479
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"We for the first time analyzed PrP-calnexin interaction."
20506117
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"The immunoprecipitation, confocal microscope and native polyacrylamide-gel electrophoresis results indicated that calnexin could bind PrP both in vitro and in vivo."
20506117
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"We were thus required to study interactions between CNX and PrP* or CNX and CD3δ separately in live cells.Since a detectable fraction of YFP-PrP* was released from the ER within 10–20 m of DNJ treatment (Fig. 5 B and Fig. S3 A), anti-flag column purification of SNAPflag-CNX from cells coexpressing SNAPflag-CNX and either CD3δ-CFP or YFP-PrP* were performed 15 m after DNJ treatment."
37702712
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"This possibility may be supported by the report that similarly to CypB, CNX interacts with PrP and reduces PrP-mediated toxicity (Wang et al., xref )."
28223916
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"The immunoprecipitation, confocal microscope and native polyacrylamide-gel electrophoresis results indicated that calnexin could bind PrP both in vitro and in vivo."
20506117
sparser
"While intriguing in itself that ER chaperones attach to mature GPI-anchored proteins, it remains unknown, however, whether such an interaction of PrP and CNX is preferred in specific membrane domains versus others."
34940479
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"These results validate the mass spectrometry findings and show that GFP-PrP* retains its associations with factors of the early secretory pathway throughout its trafficking itinerary to the lysosome.Persistent CNX interaction with PrP* after induction of ER stress was particularly surprising given the earlier finding that this interaction is lost when PrP* exits the ER during stress (Satpute-Krishnan et al., 2014)."
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