Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 1 Human Recombinant
Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 2 Human Recombinant
Dysbindin, also known as dystrobrevin-binding protein 1 (DTNBP1), is a protein that is part of the dystrophin-associated protein complex (DPC) in skeletal muscle cells. It is also a component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) . Dysbindin was initially identified through yeast two-hybrid screening for binding partners of α-dystrobrevin .
Key Biological Properties: Dysbindin is a ubiquitously expressed protein with significant roles in various cellular processes. It is involved in intracellular protein trafficking and the biogenesis of specialized organelles of the endosomal–lysosomal system .
Expression Patterns and Tissue Distribution: Dysbindin is expressed in multiple tissues, including the brain, where it is found in axon bundles and certain axon terminals, notably mossy fiber synaptic terminals in the cerebellum and hippocampus . It is also expressed in the nucleus accumbens, putamen, internal globus pallidus, caudate nucleus, hypothalamus, amygdala, cingulate gyrus, anterior cingulate cortex, substantia nigra, and other regions .
Primary Biological Functions: Dysbindin plays a crucial role in the normal physiology of the mammalian central nervous system. It is involved in transcriptional regulation, neurite and dendritic spine formation, synaptic vesicle biogenesis and exocytosis, and trafficking of glutamate and dopamine receptors .
Role in Immune Responses and Pathogen Recognition: While dysbindin’s primary functions are related to the central nervous system, its role in immune responses and pathogen recognition is not well-documented.
Mechanisms with Other Molecules and Cells: Dysbindin interacts with various molecules and cells through its involvement in the BLOC-1 complex. It binds to snapin, a protein involved in synaptic vesicle membranes, and is concentrated in synaptic vesicle membranes and postsynaptic densities .
Binding Partners and Downstream Signaling Cascades: Dysbindin’s binding partners include snapin and other proteins involved in synaptic vesicle biogenesis and exocytosis . It also interacts with members of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) superfamily, such as SNAP-25 and syntaxin 13, which control membrane fusion .
Regulatory Mechanisms Controlling Expression and Activity: Dysbindin expression and activity are regulated through various mechanisms, including transcriptional regulation and post-translational modifications. Reduced levels of dysbindin mRNA and protein have been observed in the hippocampal formation of schizophrenia patients .
Transcriptional Regulation and Post-Translational Modifications: Dysbindin is involved in the regulation of glutamatergic and dopaminergic functions through distinct mechanisms . It also plays a role in the regulation of dopamine receptor signaling pathways .
Biomedical Research: Dysbindin is a significant focus in biomedical research due to its association with schizophrenia and other neurological disorders . It is used as a target for studying the molecular mechanisms underlying these conditions.
Diagnostic Tools and Therapeutic Strategies: Dysbindin antibodies are used in diagnostic tools to study its expression and function in various tissues . Therapeutic strategies targeting dysbindin and its associated pathways are being explored for treating schizophrenia and other related disorders .
Role Throughout the Life Cycle: Dysbindin plays a critical role in neurodevelopment, with higher levels observed during embryonic and early postnatal ages than in young adulthood . It is involved in neurite outgrowth and synaptic vesicle physiology, which are essential for brain development and function .
From Development to Aging and Disease: Dysbindin’s role extends from development to aging, with its dysfunction being implicated in the pathogenesis of schizophrenia and other neurological disorders . Its involvement in intracellular protein trafficking and synaptic homeostasis is crucial for maintaining normal brain function throughout life .