Transmembrane channels

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Transmembrane channels, also called membrane channels, are pores within a lipid bilayer. The channels can be formed by protein complexes that run across the membrane or by peptides. They may cross the cell membrane, connecting the cytosol, or cytoplasm, to the extracellular matrix. [1] Transmembrane channels are also found in the membranes of organelles including the nucleus, the endoplasmic reticulum, the Golgi apparatus, mitochondria, chloroplasts, and lysosomes. [2]

Transmembrane channels differ from transporters and pumps in several ways. Some channels are less selective than typical transporters and pumps, differentiating solutes primarily by size and ionic charge. Channels perform passive transport of materials also known as facilitated diffusion. Transporters can carry out either passive or active transfer of materials while pumps require energy to act. [3]

There are several modes by which membrane channels operate. The most common is the gated channel which requires a trigger, such as a change in membrane potential in voltage-gated channels, to unlock or lock the pore opening. Voltage-gated channels are critical to the production of an action potential in neurons resulting in a nerve impulse. A ligand-gated channel requires a chemical, such as a neurotransmitter, to activate the channel. Stress-gated channels require a mechanical force applied to the channel for opening. Aquaporins are dedicated channels for the movement of water across the hydrophobic interior of the cell membrane. [4]

Ion channels are a type of transmembrane channel responsible for the passive transport of positively charged ions (sodium, potassium, calcium, hydrogen and magnesium) and negatively charged ions (chloride) and, can be either gated or ligand-gated channels. One of the best studied ion channels is the potassium ion channel. The potassium ion channel can allow rapid movement of potassium ions while being selective against sodium. Using X-ray diffraction data and atomic model computations a likely structure of the channel consists of a number of protein alpha-helixes forming an hourglass shaped pore with the narrowest point halfway through the membrane's lipid bilayer. To move through the channel the potassium ions must shed their aqueous matrix and enter a selectivity filter composed of carbonyl oxygens. The potassium ions pass through one atom at a time along five different cation (positively charged ion) binding sites. [5]

Diseases caused by ion channel malfunctions include cystic fibrosis where the channel for the chloride ion will not open or is missing in the cells of the lungs, intestine, pancreas, liver and skin. The cells can no longer regulate salt and water concentrations resulting in the symptoms typical of the disease. Additional disorders resulting from malfunctions in ion channels include forms of epilepsy, cardiac arrhythmia, certain types of periodic paralysis and ataxia. [6]

Related Research Articles

Ion channel pore-forming membrane proteins that allow the passage of ions through the membrane

Ion channels are pore-forming membrane proteins that allow ions to pass through the channel pore. Their functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by gating the flow of ions across the cell membrane, controlling the flow of ions across secretory and epithelial cells, and regulating cell volume. Ion channels are present in the membranes of all excitable cells. Ion channels are one of the two classes of ionophoric proteins, the other being ion transporters.

Integral membrane protein type of membrane protein that is permanently attached to the biological membrane

An integral membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents.

Transmembrane protein protein spanning across a biological membrane

A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

Aquaporin cellular membrane structure that selectively passes water

Aquaporins, also called water channels, are integral membrane proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. Aquaporin has six membrane-spanning alpha helical domains with both carboxylic and amino terminals on the cytoplasmic side. Two hydrophobic loops contain conserved asparagine-proline-alanine NPA motif. Because aquaporin is usually always open and is prevalent in just about every cell type, this leads to a misconception that water readily passes through the cell membrane down its concentration gradient. This is not true because only non-polar substances can diffuse directly through the lipid bilayer.

A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane protein; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion or active transport. The two main types of proteins involved in such transport are broadly categorized as either channels or carriers. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are transportome. Transportome are govern cellular influx and efflux of not only ions and nutrients but drugs as well.

Membrane potential physical quantity

Membrane potential is the difference in electric potential between the interior and the exterior of a biological cell. With respect to the exterior of the cell, typical values of membrane potential, normally given in units of millivolts and denoted as mV, ranges from –40 mV to –80 mV.

In cellular biology, membrane transport refers to the collection of mechanisms that regulate the passage of solutes such as ions and small molecules through biological membranes, which are lipid bilayers that contain proteins embedded in them. The regulation of passage through the membrane is due to selective membrane permeability - a characteristic of biological membranes which allows them to separate substances of distinct chemical nature. In other words, they can be permeable to certain substances but not to others.

Voltage-gated ion channel type of ion channel transmembrane protein

Voltage-gated ion channels are a class of transmembrane proteins that form ion channels that are activated by changes in the electrical membrane potential near the channel. The membrane potential alters the conformation of the channel proteins, regulating their opening and closing. Cell membranes are generally impermeable to ions, thus they must diffuse through the membrane through transmembrane protein channels. They have a crucial role in excitable cells such as neuronal and muscle tissues, allowing a rapid and co-ordinated depolarization in response to triggering voltage change. Found along the axon and at the synapse, voltage-gated ion channels directionally propagate electrical signals. Voltage-gated ion-channels are usually ion-specific, and channels specific to sodium (Na+), potassium (K+), calcium (Ca2+), and chloride (Cl−) ions have been identified. The opening and closing of the channels are triggered by changing ion concentration, and hence charge gradient, between the sides of the cell membrane.

Chloride channel group of transport proteins

Chloride channels are a superfamily of poorly understood ion channels specific for chloride. These channels may conduct many different ions, but are named for chloride because its concentration in vivo is much higher than other anions. Several families of voltage-gated channels and ligand-gated channels have been characterized in humans.

Inward-rectifier potassium channel group of transmembrane proteins that passively transport potassium ions

Inward-rectifier potassium channels (Kir, IRK) are a specific lipid-gated subset of potassium channels. To date, seven subfamilies have been identified in various mammalian cell types, plants, and bacteria. They are activated by phosphatidylinositol 4,5-bisphosphate (PIP2), the targets of multiple toxins, and malfunction of the channels has been implicated in several diseases. IRK channels possess a pore domain, homologous to that of voltage-gated ion channels, and flanking transmembrane segments (TMSs). They may exist in the membrane as homo- or heterooligomers and each monomer possesses between 2 and 4 TMSs. In terms of function, these proteins transport potassium (K+), with a greater tendency for K+ uptake than K+ export. The process of inward-rectification was discovered by Denis Noble in cardiac muscle cells in 1960s and by Richard Adrian and Alan Hodgkin in 1970 in skeletal muscle cells.

Voltage-gated potassium channel InterPro Family

Voltage-gated potassium channels (VGKCs) are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential. During action potentials, they play a crucial role in returning the depolarized cell to a resting state.

Light-gated ion channels are a family of ion channels regulated by electromagnetic radiation. Other gating mechanisms for ion channels include voltage-gated ion channels, ligand-gated ion channels, mechanosensitive ion channels, and temperature-gated ion channels. Most light-gated ion channels have been synthesized in the laboratory for study, although two naturally occurring examples, channelrhodopsin and anion-conducting channelrhodopsin, are currently known. Photoreceptor proteins, which act in a similar manner to light-gated ion channels, are generally classified instead as G protein-coupled receptors.

Major intrinsic proteins group of ion channel proteins that function in water, small carbohydrate (e.g., glycerol), urea, NH3, CO2, H2O2 and ion transport by energy-independent mechanisms

Major intrinsic proteins comprise a large superfamily of transmembrane protein channels that are grouped together on the basis of homology. The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins.

  1. The aquaporins (AQPs) are water selective.
  2. The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol.
  3. The third subfamily, with little conserved amino acid sequences around the NPA boxes, include 'superaquaporins' (S-aquaporins).
Channel blocker molecule able to block protein channels, frequently used as pharmaceutical

A channel blocker is the biological mechanism in which a particular molecule is used to prevent the opening of ion channels in order to produce a physiological response in a cell. Channel blocking is conducted by different types of molecules, such as cations, anions, amino acids, and other chemicals. These blockers act as ion channel antagonists, preventing the response that is normally provided by the opening of the channel.

Mechanosensitive channels, mechanosensitive ion channels or stretch-gated ion channels (not to be confused with mechanoreceptors). They are present in the membranes of organisms from the three domains of life: bacteria, archaea, and eukarya. They are the sensors for a number of systems including the senses of touch, hearing and balance, as well as participating in cardiovascular regulation and osmotic homeostasis (e.g. thirst). The channels vary in selectivity for the permeating ions from nonselective between anions and cations in bacteria, to cation selective allowing passage Ca2+, K+ and Na+ in eukaryotes, and highly selective K+ channels in bacteria and eukaryotes.

Gating (electrophysiology)

In electrophysiology, the term gating refers to the opening (activation) or closing of ion channels. This change in conformation is a response to changes in transmembrane voltage.

Synthetic ion channels

Synthetic ion channels are de novo chemical compounds that insert into lipid bilayers, form pores, and allow ions to flow from one side to the other. They are man-made analogues of natural ion channels, and are thus also known as artificial ion channels. Compared to biological channels, they usually allow fluxes of similar magnitude but are

  1. minuscule in size,
  2. diverse in molecular architecture, and
  3. may rely on diverse supramolecular interactions to pre-form the active, conducting structures.
Cell membrane Biological membrane that separates the interior of a cell from its outside environment

The cell membrane is a biological membrane that separates the interior of all cells from the outside environment which protects the cell from its environment. Cell membrane consists of a lipid bilayer, including cholesterols that sit between phospholipids to maintain their fluidity under various temperature, in combination with membrane proteins such as integral proteins, and peripheral proteins that go across inside and outside of the membrane serving as membrane transporter, and loosely attached to the outer (peripheral) side of the cell membrane acting as several kinds of enzymes shaping the cell, respectively. The cell membrane controls the movement of substances in and out of cells and organelles. In this way, it is selectively permeable to ions and organic molecules. In addition, cell membranes are involved in a variety of cellular processes such as cell adhesion, ion conductivity and cell signalling and serve as the attachment surface for several extracellular structures, including the cell wall, the carbohydrate layer called the glycocalyx, and the intracellular network of protein fibers called the cytoskeleton. In the field of synthetic biology, cell membranes can be artificially reassembled.

This is a list of articles on biophysics.

KcsA potassium channel prokaryotic potassium ion channel

KcsA (Kchannel of streptomyces A) is a prokaryotic potassium channel from the soil bacteria Streptomyces lividans that has been studied extensively in ion channel research. The pH activated protein possesses two transmembrane segments and a highly selective pore region, responsible for the gating and shuttling of K+ ions out of the cell. The amino acid sequence found in the selectivity filter of KcsA is highly conserved among both prokaryotic and eukaryotic K+ voltage channels; as a result, research on KcsA has provided important structural and mechanistic insight on the molecular basis for K+ ion selection and conduction. As one of the most studied ion channels to this day, KcsA is a template for research on K+ channel function and its elucidated structure underlies computational modeling of channel dynamics for both prokaryotic and eukaryotic species.

References

  1. ↑ Roux, B., and Schulten, K. (2004). Computationals Studies of Membrane Channels. Structure 12, 1343 - 1351.
  2. ↑ Alberts, B., Bray, D., Hopkin, K., and Johnson, A. (2010) Essential Cell Biology, 3rd ed. (New York: Garland Science) pp. 387 – 420.
  3. ↑ Lodish, H., Berk, A., Kaiser, C., Krieger, M., Scott, M., Bretscher, A., Ploegh, H., and Matsudaira, P. (2008) Molecular Cell Biology, 6th ed. (New York: W. H. Freeman) pp. 437 – 474.
  4. ↑ Verkman, A. (2011) Aquaporins at a Glance. Journal of Cell Science 24, 2107 - 2112.
  5. ↑ Roux, B., and Schulten, K. (2004). Computationals Studies of Membrane Channels. Structure 12, 1343 - 1351.
  6. ↑ Celesia, G. G. (2001) Disorders of Membrane Channels or Channelopathies. Clinical Neurophysiology Jan, 112 (1), 2 - 18.
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