Related Experiment Video
Updated: Nov 9, 2025
10:46
Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
Published on: July 16, 2013
16.5K
Structure versus function: Are new conformations of pannexin 1 yet to be resolved?
Carsten Mim1, Guy Perkins2, Gerhard Dahl3
1Department of Biomedical Engineering and Health Systems Royal Institute of Technology, Huddinge, Sweden.
The Journal of General Physiology
|April 9, 2021
Summary
Pannexin 1 (Panx1) channels are crucial for many bodily functions, but their exact structure and role in ATP release remain unclear. Further research is needed to determine the Panx1 conformation responsible for ATP permeation.
Area of Science:
- Molecular biology
- Cell physiology
- Biophysics
Background:
- Pannexin 1 (Panx1) is implicated in diverse physiological and pathological processes.
- Panx1 is primarily known for its role in purinergic signaling via ATP release.
- Recent structural studies of Panx1 channels have emerged.
Purpose of the Study:
- To critically evaluate the existing evidence for Panx1 channel structure and function.
- To address the discrepancy between structural data and the proposed ATP release function of Panx1.
- To identify future research directions for elucidating Panx1 channel mechanisms.
Main Methods:
- Critical assessment of current scientific literature.
- Analysis of recent structural data on Panx1 channels.
- Comparative analysis of functional and structural evidence.
Main Results:
- Existing Panx1 channel structures are consistent with chloride selectivity, not ATP release.
- No determined Panx1 conformation strongly supports its role as an ATP release pathway.
- The precise structure facilitating ATP permeation remains elusive.
Conclusions:
- The structure enabling ATP release through Panx1 has not yet been determined.
- Further investigation is required to understand the Panx1 channel's diverse functions.
- Strategies are proposed to achieve the large-pore, ATP-permeable Panx1 conformation.
Related Concept Videos
01:37Gap Junctions
55.7K
Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
55.7K
01:27Gap Junctions
8.8K
The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
8.8K
01:21Structure of Porins
3.5K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.5K
01:09Multi-pass Transmembrane Proteins and β-barrels
6.0K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.0K
01:25Aquaporins
5.7K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
5.7K
01:23Catenins
2.7K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
2.7K