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OFP

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OFP

Re: MycroftHolmes post# 103172

Thursday, 04/27/2017 6:33:32 AM

Thursday, April 27, 2017 6:33:32 AM

Post# of 458207

the Sigma Receptor does not impact protein folding directly by chaperoning but rather indirectly but modulating PERK, IRE1a, and ATF6 and thus the UPR (Unfolded Protein Response)

The modulation pathways is correct.

Its nicely explained here: Role of sigma-1 receptors in neurodegenerative diseases

Though this is considered a chaperone function: "As chaperones, sigma-1 receptors can modulate the UPR. In its dormant state, the sigma-1 receptor forms a complex at the MAM with the ER chaperone and signaling regulator BiP/Grp78 (4). During ER stress or via ligand stimulation, sigma-1 receptors dissociate from BiP/Grp78 and can modulate the activity of other proteins, including PERK, IRE1a, and ATF6 (4)" same ref.

More explicitly:

Sigma-1 Receptor Chaperones and Diseases
Shang-Yi Tsai, Teruo Hayashi, Tomohisa Mori, and Tsung-Ping Su*

Abstract
Chaperones are proteins that assist the correct folding of other protein clients either when the clients are being synthesized or at their functional localities...



In reference to your misquote... I had said modulation of protein folding was "one of the main" chaperone functions...you had quoted it as "the main" chaperone function. Not worth mentioning had someone not tried to leverage the distinction.
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