Rxivist logo

Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 73,086 bioRxiv papers from 318,192 authors.

Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2 (PC2)

By Qinrui Wang, George Hedger, Prafulla Aryal, Mariana Grieben, Chady Nasrallah, Agnese Baronina, Ashley CW Pike, Jiye Shi, Elisabeth P Carpenter, Mark S. P. Sansom

Posted 26 Mar 2019
bioRxiv DOI: 10.1101/589515 (published DOI: 10.1016/j.str.2019.11.005)

Polycystin-2 (PC2) is a member of the TRPP subfamily of TRP channels and is present in ciliary membranes of the kidney. PC2 can be either homo-tetrameric, or heterotetrameric with PC1. PC2 shares a common transmembrane fold with other TRP channels, in addition to having a novel extracellular domain. Several TRP channels have been suggested to be regulated by lipids, including phosphatidylinositol phosphates (PIPs). We have combined molecular dynamics simulations with cryoelectron microscopy to explore possible lipid interactions sites on PC2. We propose that PC2 has a PIP-binding site close to the equivalent vanilloid/lipid-binding site in the TRPV1 channel. A 3.0 Å cryoelectron microscopy map reveals a binding site for cholesterol on PC2. Cholesterol interactions with the channel at this site are further characterized by MD simulations. These results help to position PC2 within an emerging model of the complex roles of lipids in the regulation and organization of ciliary membranes.

Download data

  • Downloaded 464 times
  • Download rankings, all-time:
    • Site-wide: 26,064 out of 73,086
    • In biophysics: 989 out of 3,105
  • Year to date:
    • Site-wide: 25,553 out of 73,086
  • Since beginning of last month:
    • Site-wide: 25,553 out of 73,086

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News