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Synucleins are a family of soluble proteins predominantly found in vertebrates. They are primarily expressed in neural tissue and certain tumors. The family includes three members: alpha-synuclein, beta-synuclein, and gamma-synuclein. The name “synuclein” is derived from their initial discovery in the synapses and nuclei of neurons . Alpha-synuclein is the most studied member due to its association with neurodegenerative diseases such as Parkinson’s disease .
Key Biological Properties: Alpha-synuclein is a small protein composed of 140 amino acids. It is known for its ability to adopt various conformational states, which is crucial for its function and aggregation properties .
Expression Patterns: Alpha-synuclein is abundantly expressed in the brain, particularly in the neocortex, hippocampus, substantia nigra, thalamus, and cerebellum . It is also present in the peripheral nervous system, muscle, liver, heart, lungs, kidney, hematopoietic cells of the bone marrow, and circulating blood cells .
Tissue Distribution: While alpha-synuclein is most abundant in neural tissues, smaller amounts are found in the heart, muscle, and other tissues . Beta-synuclein is primarily located at presynaptic terminals in the central nervous system, and gamma-synuclein is mainly expressed in the peripheral nervous system, ocular, and adipose tissues .
Primary Biological Functions: Alpha-synuclein plays a critical role in regulating synaptic vesicle trafficking and neurotransmitter release . It is involved in neurotransmission, calcium homeostasis, mitochondrial function, and gene regulation .
Role in Immune Responses and Pathogen Recognition: Although the primary focus has been on its role in the nervous system, recent studies suggest that alpha-synuclein may also play a role in immune responses and pathogen recognition. However, more research is needed to fully understand these functions .
Mechanisms with Other Molecules and Cells: Alpha-synuclein interacts with phospholipids and proteins within presynaptic terminals. It binds to phospholipids of the plasma membrane via its N-terminus domain and to synaptobrevin-2 via its C-terminus domain, which is crucial during synaptic activity .
Binding Partners and Downstream Signaling Cascades: Alpha-synuclein functions as a molecular chaperone in the formation of SNARE complexes, which are essential for synaptic vesicle fusion and neurotransmitter release . It also interacts with other proteins and lipids, influencing various signaling pathways .
Transcriptional Regulation: The expression of alpha-synuclein is controlled by several mechanisms, including transcriptional regulation. It binds to DNA and histones, participating in epigenetic regulatory functions that control specific gene transcription .
Post-Translational Modifications: Alpha-synuclein undergoes various post-translational modifications, such as phosphorylation, ubiquitination, and acetylation, which regulate its function and aggregation properties .
Biomedical Research: Alpha-synuclein is extensively studied in the context of neurodegenerative diseases, particularly Parkinson’s disease. Understanding its role in these diseases can lead to the development of new therapeutic strategies .
Diagnostic Tools: Alpha-synuclein can serve as a biomarker for the early diagnosis of neurodegenerative diseases. Techniques such as real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification (PMCA) are used to detect pathological alpha-synuclein in peripheral tissues .
Therapeutic Strategies: Targeting alpha-synuclein aggregation and its interactions with other molecules is a promising approach for developing disease-modifying therapies for Parkinson’s disease and other synucleinopathies .
Development to Aging and Disease: Alpha-synuclein plays a role throughout the life cycle, from development to aging. During development, it is involved in synaptic formation and plasticity. In aging and disease, its aggregation into Lewy bodies is a hallmark of neurodegenerative diseases such as Parkinson’s disease and dementia with Lewy bodies .