Transporter Cell Lines
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
Background of Membrane Transporter
Transport proteins constitute a subclass of cell membrane proteins. Transport proteins can be found on the surface of almost any cell, bacteria, or virus, and are mainly responsible for the entry and exit of ions, small molecules, macromolecules, and others. They can be further grouped into several subclasses according to the differences in functions and structures, denoted as channels and pores, porters, and pumps.
Fig.1 Structure Prediction of MDR1, a member of ABC multidrug transporter. (Uniprot ID A0A095C325; obtained from Alphafold)
Functions and Mechanisms of Membrane Transporter
The cytoplasmic membrane is composed of a complete and impermeable phospholipid bilayer, which ensures the integrity of the cell and resists harmful substances outside the cell. However, some essential ions and molecules are critical for maintaining cellular homeostasis, and the transport of these ions and molecules is the most important and basic function of transport proteins. On the membrane of the same cell, although it can be activated by a variety of upstream signals, every transport protein can only specifically transport a certain type of molecule or ion. The transporter proteins of different subgroups mainly realize the transmembrane transport of substances through three mechanisms, namely active transport, diffusion, and reverse diffusion.
Application and Pathology of Transporter Cell Lines
The dysfunction and distribution of cell membrane transport protein may lead to various diseases and disorders in organisms, including neurological diseases, endocrine disorders, genetic diseases, or cancer. Besides, transport proteins are responsible for drug delivery and biomacromolecule transport in cells, therefore, transport proteins may represent ideal targets for therapeutic or clinical intervention in a wide variety of diseases.
Published Data
| Paper Title | Evolution of the membrane transport protein domain |
| Journal | International Journal of Molecular Sciences |
| Published | 2022 |
| Abstract | Membrane transporters are ubiquitously present in all organisms, but their functions, transport substrates, and mechanisms of action remain unclear. Here, the researchers used different bioinformatics tools to study the evolution of membrane transport proteins (MTPs), analyze the regional organization and ring topology, and study the comparative alignment of the modeled 3D structures. The results showed that MTPs from different taxa were highly conserved at both amino acid and structural levels, implying a certain degree of functional similarity. The presence of loops of varying lengths at different positions indicates tax adaptation to transported substrates, intracellular localization, accessibility to post-translational modifications, and interactions with other proteins. The comparison of model structures reveals that MTP and Na/H exchangers are closely related and share a common origin. Furthermore, the high amino acid similarity and identity between archaeal and bacterial MTPs and Na/H exchangers implies that the ion transport function is conserved, at least for archaeal and bacterial MTPs. |
| Result |
Investigators provide a phylogenetic and structural analysis of membrane transporter domains. Phylogenetic findings revealed the existence of 13 primary clades and identified several gene transfer events that may have occurred between distant taxa. Transmembrane domain composition analysis revealed no conservation in TM domains III, V, and X, whereas other TM domains were conserved in all taxa studied. The presence of cytoplasmic and non-cytoplasmic loops of different lengths and locations indicates the adaptation of the species to transport substrates, intracellular localization, and potential protein-protein interactions. The comparison of the model structures revealed a high degree of conservation among MTP domains from different taxa. Furthermore, the high structural similarity between archaeal and bacterial MTPs and Na/H exchangers implies a close functional link, possibly a similarity in transport substrates. Further experimental data on the function and physiological role of MTP in other taxa such as fungi, bacteria, archaea, and animals will help to understand the structure-function relationship and its evolutionary significance.
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Fig.2 Alignment of structural models of proteins containing MTP domains from different taxa. (Dabravolski, 2022)
Reference
- Dabravolski, S.A.; et al. Evolution of the membrane transport protein domain. International Journal of Molecular Sciences. 2022, 23: 8094.
