Related Experiment Video

Updated: Jul 16, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
12:09

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

10.2K

Intrinsically disordered regions in TRPV2 mediate protein-protein interactions

Raghavendar R Sanganna Gari1, Grigory Tagiltsev1, Ruth A Pumroy2,3

  • 1Department of Anesthesiology, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.

Communications Biology
|September 22, 2023
PubMed

Insights

Intrinsically disordered regions (IDRs) of TRPV2 channels are essential for function. High-speed atomic force microscopy visualized these TRPV2 IDRs, revealing their role in protein-protein interactions.

Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Biology

Background:

  • Transient receptor potential (TRP) ion channels regulate cellular processes and somatosensation via cation influx.
  • While most TRP channel structures are known, ~30% of their sequences, primarily termini, are intrinsically disordered regions (IDRs) with poorly understood roles.
  • IDRs are crucial for native TRP channel function, yet their structure, dynamics, and specific functions remain largely unelucidated.

Purpose of the Study:

  • To investigate the structure, dynamics, and function of intrinsically disordered regions (IDRs) in TRPV2 ion channels.
  • To visualize IDRs in native TRPV2 channels using high-speed atomic force microscopy (HS-AFM).
  • To elucidate the role of TRPV2 IDRs in intermolecular interactions and channel function.

Main Methods:

  • High-speed atomic force microscopy (HS-AFM) for dynamic single-molecule imaging of TRPV2 channels in membranes.
  • Structural and sequence analysis of TRP channel sequences, focusing on intrinsically disordered regions (IDRs).

Main Results:

  • HS-AFM successfully visualized TRPV2 channels in membranes, capturing dynamic behavior.
  • The study revealed that N-terminal intrinsically disordered regions (IDRs) of TRPV2 are involved in intermolecular interactions.
  • Evidence was provided for the 'structure' and dynamics of TRPV2 IDRs, suggesting their role in mediating protein-protein interactions.

Conclusions:

  • Intrinsically disordered regions (IDRs) of TRPV2 ion channels possess a discernible 'structure' and dynamics in membranes.
  • N-terminal IDRs of TRPV2 channels play a significant role in mediating protein-protein interactions.
  • These findings advance the understanding of IDR function in TRP channel regulation and molecular interactions.

More Related Videos

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.1K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

1.8K

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
4.7K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

3.8K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K