Intrinsically disordered regions in TRPV2 mediate protein-protein interactions.

TitleIntrinsically disordered regions in TRPV2 mediate protein-protein interactions.
Publication TypeJournal Article
Year of Publication2023
AuthorsGari RRSanganna, Tagiltsev G, Pumroy RA, Jiang Y, Blackledge M, Moiseenkova-Bell VY, Scheuring S
JournalCommun Biol
Date Published2023 Sep 22
KeywordsIntrinsically Disordered Proteins, Microscopy, Atomic Force, Single Molecule Imaging, TRPV Cation Channels

Transient receptor potential (TRP) ion channels are gated by diverse intra- and extracellular stimuli leading to cation inflow (Na+, Ca2+) regulating many cellular processes and initiating organismic somatosensation. Structures of most TRP channels have been solved. However, structural and sequence analysis showed that ~30% of the TRP channel sequences, mainly the N- and C-termini, are intrinsically disordered regions (IDRs). Unfortunately, very little is known about IDR 'structure', dynamics and function, though it has been shown that they are essential for native channel function. Here, we imaged TRPV2 channels in membranes using high-speed atomic force microscopy (HS-AFM). The dynamic single molecule imaging capability of HS-AFM allowed us to visualize IDRs and revealed that N-terminal IDRs were involved in intermolecular interactions. Our work provides evidence about the 'structure' of the TRPV2 IDRs, and that the IDRs may mediate protein-protein interactions.

Alternate JournalCommun Biol
PubMed ID37736816
PubMed Central IDPMC10516966
Grant ListR01 NS110790 / NS / NINDS NIH HHS / United States
DP1 AT010874 / AT / NCCIH NIH HHS / United States
R35 GM144120 / GM / NIGMS NIH HHS / United States
R01 GM103899 / GM / NIGMS NIH HHS / United States