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=''>
<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 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>.  


== Function ==
== 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 10.1101/cshperspect.a009399</ref>.
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>.