Sandbox Reserved 1109: Difference between revisions

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α-synuclein is a protein encoded by the SNCA gene in humans and belongs to the family of synuclein proteins that also consist of beta and gamma- synuclein. It is present in large quantities in the brain and in comparatively smaller quantities in other tissues in the body. α-synuclein is mainly present at the presynaptic terminals in the neuronal mitochondria and ~~comprises~~ of 1% of the total cytosolic protein in the nervous system. It is ~~mainly related~~ to neurodegenerative diseases in humans <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.

α-synuclein is a protein encoded by the SNCA gene in humans and belongs to the family of synuclein proteins that also consist of beta and gamma- synuclein. It is present in large quantities in the brain and in comparatively smaller quantities in other tissues in the body. α-synuclein is mainly present at the presynaptic terminals in the neuronal mitochondria and consists of 1% of the total cytosolic protein in the nervous system. Recently, it became evident that α-synuclein is directly linked to neurodegenerative diseases in humans <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.

== Function ==

Even though it is well known that the aggregation of ~~this protein~~ is related to neurodegenerative disorders, the ~~regular~~ function of the protein ~~is not well understood~~. ~~However~~, the literature suggests that there exists a strong genetic link between ~~the protein~~ and degeneration that arises from the loss of certain chaperone proteins, called presynaptic chaperone cysteine string proteins (CSPα). This loss of CSPα does not affect the transmission of the neuronal signals immediately but progresses ~~with~~ time. ~~Excessive~~ expression of α-synuclein is noted to delay degeneration that happens due to loss of CSPα, ~~thus giving~~ α-synuclein a chaperone-like function where ~~this protein~~ works with the CSPα in the assembly of the SNARE complex, ~~which~~ is a ~~type of~~ large protein complex that ~~deals with~~ the fusion synaptic vesicles with the neurons in the brain. ~~Therefore it is~~ said ~~that~~ the ~~main function~~ of ~~the~~ α-synuclein is to ~~regulate~~ the neurotransmitter release <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.

Even though it is well known that the aggregation of α-synuclein is related to neurodegenerative disorders, the actual function of the protein remains unknown. Nonetheless, the literature suggests that there exists a strong genetic link between α-synuclein and synaptic degeneration that arises from the loss of certain chaperone proteins called presynaptic chaperone cysteine string proteins (CSPα). This loss of CSPα does not affect the transmission of the neuronal signals immediately but progresses over time. However, excessive expression of α-synuclein is noted to delay synaptic degeneration that happens due to the loss of CSPα. As a result, α-synuclein is suggested to have a chaperone-like function, where it works with the CSPα in the assembly of the SNARE complex. More precisely, the latter is a large protein complex that is responsible for the fusion of synaptic vesicles with the neurons in the brain. That being said, there are exist several hypotheses around the role of α-synuclein protein, but studies suggest that its function is related to the regulation of synaptic vesicles, which in turn reduce the effect of synaptic recycling and neurotransmitter release <ref>DOI 10.1016/j.neuron.2013.09.004</ref><ref> DOI: 10.1016/j.neuron.2009.12.023</ref>.

Sandbox Reserved 1109: Difference between revisions

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 <StructureSection load='6flt' size='340' side='right'caption='[[6flt]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
-α-synuclein is a protein encoded by the SNCA gene in humans and belongs to the family of synuclein proteins that also consist of beta and gamma- synuclein. It is present in large quantities in the brain and in comparatively smaller quantities in other tissues in the body. α-synuclein is mainly present at the presynaptic terminals in the neuronal mitochondria and comprises of 1% of the total cytosolic protein in the nervous system. It is mainly related to neurodegenerative diseases in humans <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.
+α-synuclein is a protein encoded by the SNCA gene in humans and belongs to the family of synuclein proteins that also consist of beta and gamma- synuclein. It is present in large quantities in the brain and in comparatively smaller quantities in other tissues in the body. α-synuclein is mainly present at the presynaptic terminals in the neuronal mitochondria and consists of 1% of the total cytosolic protein in the nervous system. Recently, it became evident that α-synuclein is directly linked to neurodegenerative diseases in humans <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.
 == Function ==
-Even though it is well known that the aggregation of this protein is related to neurodegenerative disorders, the regular function of the protein is not well understood. However, the literature suggests that there exists a strong genetic link between the protein and degeneration that arises from the loss of certain chaperone proteins, called presynaptic chaperone cysteine string proteins (CSPα). This loss of CSPα does not affect the transmission of the neuronal signals immediately but progresses with time. Excessive expression of α-synuclein is noted to delay degeneration that happens due to loss of CSPα, thus giving α-synuclein a chaperone-like function where this protein works with the CSPα in the assembly of the SNARE complex, which is a type of large protein complex that deals with the fusion synaptic vesicles with the neurons in the brain. Therefore it is said that the main function of the α-synuclein is to regulate the neurotransmitter release <ref>DOI 10.1016/j.neuron.2013.09.004</ref>.
+Even though it is well known that the aggregation of α-synuclein is related to neurodegenerative disorders, the actual function of the protein remains unknown. Nonetheless, the literature suggests that there exists a strong genetic link between α-synuclein and synaptic degeneration that arises from the loss of certain chaperone proteins called presynaptic chaperone cysteine string proteins (CSPα). This loss of CSPα does not affect the transmission of the neuronal signals immediately but progresses over time. However, excessive expression of α-synuclein is noted to delay synaptic degeneration that happens due to the loss of CSPα. As a result, α-synuclein is suggested to have a chaperone-like function, where it works with the CSPα in the assembly of the SNARE complex. More precisely, the latter is a large protein complex that is responsible for the fusion of synaptic vesicles with the neurons in the brain. That being said, there are exist several hypotheses around the role of α-synuclein protein, but studies suggest that its function is related to the regulation of synaptic vesicles, which in turn reduce the effect of synaptic recycling and neurotransmitter release <ref>DOI 10.1016/j.neuron.2013.09.004</ref><ref> DOI: 10.1016/j.neuron.2009.12.023</ref>.