Vesicular Neurotransmitter Transport Proteins
Neurotransmitter Transport Proteins
Plasma Membrane Neurotransmitter Transport Proteins
Vesicular Monoamine Transport Proteins
Vesicular Glutamate Transport Proteins
Vesicular Biogenic Amine Transport Proteins
Synaptic Vesicles
Vesicular monogamy? (1/8)
Vesicular neurotransmitter transporters package transmitter into the lumen of synaptic vesicles for quantal release. However, the number of transporters that localize to each vesicle is not known. In this issue of Neuron, a study by Daniels et al. using the Drosophila neuromuscular junction and mutations of the vesicular glutamate transporter suggests that one transporter may suffice to fill each vesicle. (+info)Vesicular glutamate (VGlut), GABA (VGAT), and acetylcholine (VACht) transporters in basal forebrain axon terminals innervating the lateral hypothalamus. (2/8)
The basal forebrain (BF) is known to play important roles in cortical activation and sleep, which are likely mediated by chemically differentiated cell groups including cholinergic, gamma-aminobutyric acid (GABA)ergic and other unidentified neurons. One important target of these cells is the lateral hypothalamus (LH), which is critical for arousal and the maintenance of wakefulness. To determine whether chemically specific BF neurons provide an innervation to the LH, we employed anterograde transport of 10,000 MW biotinylated dextran amine (BDA) together with immunohistochemical staining of the vesicular transporter proteins (VTPs) for glutamate (VGluT1, -2, and -3), GABA (VGAT), or acetylcholine (ACh, VAChT). In addition, we applied triple staining for the postsynaptic proteins (PSPs), PSD-95 with VGluT or Gephyrin (Geph) with VGAT, to examine whether the BDA-labeled varicosities may form excitatory or inhibitory synapses in the LH. Axons originating from BDA-labeled neurons in the magnocellular preoptic nucleus (MCPO) and substantia innominata (SI) descended within the medial forebrain bundle and extended collateral varicose fibers to contact LH neurons. In the LH, the BDA-labeled varicosities were immunopositive (+) for VAChT ( approximately 10%), VGluT2 ( approximately 25%), or VGAT ( approximately 50%), revealing an important influence of newly identified glutamatergic together with GABAergic BF inputs. Moreover, in confocal microscopy, VGluT2+ and VGAT+ terminals were apposed to PSD-95+ and Geph+ profiles respectively, indicating that they formed synaptic contacts with LH neurons. The important inputs from glutamatergic and GABAergic BF cells could thus regulate LH neurons in an opposing manner to stimulate vs. suppress cortical activation and behavioral arousal reciprocally. (+info)An Arf-like small G protein, ARL-8, promotes the axonal transport of presynaptic cargoes by suppressing vesicle aggregation. (3/8)
(+info)Vesicular neurotransmitter transporter trafficking in vivo: moving from cells to flies. (4/8)
(+info)Divalent cation transport by vesicular nucleotide transporter. (5/8)
(+info)Neurotransmitter corelease: mechanism and physiological role. (6/8)
(+info)Sources contributing to the average extracellular concentration of dopamine in the nucleus accumbens. (7/8)
(+info)Intracellular Ca2+ stores and Ca2+ influx are both required for BDNF to rapidly increase quantal vesicular transmitter release. (8/8)
(+info)Vesicular neurotransmitter transport proteins are a type of membrane protein that play a crucial role in the storage and release of neurotransmitters within neurons. They are responsible for transporting neurotransmitters from the cytoplasm into synaptic vesicles, which are small membrane-bound sacs that store neurotransmitters and are released during neurotransmission.
There are several different types of vesicular neurotransmitter transport proteins, each specific to a particular neurotransmitter or group of neurotransmitters. For example, the vesicular monoamine transporter (VMAT) family transports monoamines such as dopamine, norepinephrine, and serotonin, while the vesicular acetylcholine transporter (VAChT) transports acetylcholine.
These transport proteins are critical for maintaining appropriate levels of neurotransmitters in the synapse and regulating neuronal signaling. Dysfunction in these proteins has been implicated in a variety of neurological disorders, including Parkinson's disease, depression, and attention deficit hyperactivity disorder (ADHD).
Neurotransmitter transport proteins are a type of membrane transporter protein that are responsible for the reuptake of neurotransmitters from the synaptic cleft back into the presynaptic neuron or glial cells. These proteins play a crucial role in regulating the concentration and duration of action of neurotransmitters in the synapse, thereby terminating the neurotransmission process.
There are two main types of neurotransmitter transport proteins: sodium-dependent and sodium-independent transporters. Sodium-dependent transporters use the energy generated by the movement of sodium ions across the membrane to transport neurotransmitters against their concentration gradient, while sodium-independent transporters do not require sodium ions for transport.
Neurotransmitter transport proteins are specific to each type of neurotransmitter and play an essential role in maintaining the homeostasis of the nervous system. Dysfunction of these proteins has been implicated in various neurological and psychiatric disorders, such as depression, anxiety, and Parkinson's disease.
Plasma membrane neurotransmitter transport proteins are a type of transmembrane protein found in the plasma membrane of neurons and other cells. They are responsible for the active transport of neurotransmitters, which are chemical messengers that transmit signals between neurons, from the extracellular space into the cell. This process helps to terminate the signal transmission and regulate the concentration of neurotransmitters in the synaptic cleft, which is the narrow gap between the presynaptic and postsynaptic neurons.
There are two main types of plasma membrane neurotransmitter transport proteins: sodium-dependent transporters and sodium-independent transporters. Sodium-dependent transporters use the energy generated by the movement of sodium ions across the membrane to move neurotransmitters against their concentration gradient, while sodium-independent transporters do not require sodium ions and use other sources of energy.
These transport proteins play a crucial role in maintaining the homeostasis of neurotransmitter levels in the brain and are targets for many drugs used to treat neurological and psychiatric disorders, such as antidepressants, antipsychotics, and stimulants.
Vesicular Monoamine Transporter Proteins (VMATs) are a type of transmembrane protein that play a crucial role in the packaging and transport of monoamines, such as serotonin, dopamine, and norepinephrine, into synaptic vesicles within neurons. There are two main isoforms of VMATs, VMAT1 and VMAT2, which differ in their distribution and function.
VMAT1 (also known as SLC18A1) is primarily found in neuroendocrine cells and is responsible for transporting monoamines into large dense-core vesicles. VMAT2 (also known as SLC18A2), on the other hand, is mainly expressed in presynaptic neurons and is involved in the transport of monoamines into small synaptic vesicles.
Both VMAT1 and VMAT2 are integral membrane proteins that utilize a proton gradient to drive the uptake of monoamines against their concentration gradient, allowing for their storage and subsequent release during neurotransmission. Dysregulation of VMAT function has been implicated in several neurological and psychiatric disorders, including Parkinson's disease and depression.
Vesicular Glutamate Transport Proteins (VGLUTs) are a group of proteins that play a crucial role in the packaging and transport of the neurotransmitter glutamate into synaptic vesicles within neurons. Glutamate is the primary excitatory neurotransmitter in the central nervous system, and its release and uptake must be tightly regulated to maintain proper neural communication.
VGLUTs are integral membrane proteins located on the membranes of synaptic vesicles. They facilitate the accumulation of glutamate inside these vesicles through a process called antiport, where they exchange glutamate for protons from the cytoplasm. This results in a high concentration of glutamate within the vesicle, allowing for its regulated release upon neuronal stimulation.
There are three isoforms of VGLUTs (VGLUT1, VGLUT2, and VGLUT3) encoded by different genes (SLC17A7, SLC17A6, and SLC17A8, respectively). These isoforms exhibit distinct expression patterns in the central nervous system and are involved in various neurological functions. Dysregulation of VGLUTs has been implicated in several neurological disorders, including epilepsy, pain perception, and neurodegenerative diseases.
Vesicular biogenic amine transport proteins (VMATs) are a type of transmembrane protein that play a crucial role in the packaging and transport of biogenic amines, such as serotonin, dopamine, norepinephrine, and histamine, into synaptic vesicles within neurons. These proteins are located on the membranes of neurosecretory vesicles and function to regulate the concentration of these neurotransmitters in the cytoplasm and maintain their storage in vesicles until they are released into the synapse during neurotransmission. VMATs are members of the solute carrier family 18 (SLC18) and consist of two isoforms, VMAT1 and VMAT2, which differ in their distribution and substrate specificity. VMAT1 is primarily found in non-neuronal cells, such as endocrine and neuroendocrine cells, while VMAT2 is predominantly expressed in neurons. Dysregulation of VMATs has been implicated in several neurological and psychiatric disorders, including Parkinson's disease, depression, and attention deficit hyperactivity disorder (ADHD).
Synaptic vesicles are tiny membrane-enclosed sacs within the presynaptic terminal of a neuron, containing neurotransmitters. They play a crucial role in the process of neurotransmission, which is the transmission of signals between nerve cells. When an action potential reaches the presynaptic terminal, it triggers the fusion of synaptic vesicles with the plasma membrane, releasing neurotransmitters into the synaptic cleft. These neurotransmitters can then bind to receptors on the postsynaptic neuron and trigger a response. After release, synaptic vesicles are recycled through endocytosis, allowing them to be refilled with neurotransmitters and used again in subsequent rounds of neurotransmission.