Fig. 10: The TRPV4 IDR forms an extensive ‘belt’ along the membrane plane and encodes a hierarchy of antagonistic regulatory modules. | Nature Communications

Fig. 10: The TRPV4 IDR forms an extensive ‘belt’ along the membrane plane and encodes a hierarchy of antagonistic regulatory modules.

From: Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity

Fig. 10: The TRPV4 IDR forms an extensive ‘belt’ along the membrane plane and encodes a hierarchy of antagonistic regulatory modules.The alternative text for this image may have been generated using AI.

a, b Superimposed IDR conformations from coarse-grained MD simulations (pink licorice) integrated into a full-length TRPV4 tetramer (AlphaFold94 prediction of G. gallus TRPV4 transmembrane core (gray) and ARDs (cyan)) viewed from the side a and from the intracellular side b. For better visualization of the extent of the IDR ‘belt’, the IDR conformations of the front facing TRPV4 monomer have been deleted. For a view of the IDR conformations on a single TRPV4 subunit, see Supplementary Fig. 13 as well as Supplementary Movies 2 and 3. c The TRPV4 N-terminus encodes multiple antagonistic regulatory elements that regulate TRPV4 function through ligand, protein, lipid or intra-domain contacts. d PIP2-binding site interactions with the membrane exert a pull force on the IDR C-terminus. Likewise, pulling on the IDR can lead to membrane deformation. Crosstalk between the PIP2-binding site and the autoinhibitory patch modulates PIP2 binding and thus IDR membrane interactions, thereby influencing channel activity.

Back to article page