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Autoimmune thyroid disorders, including Hashimoto's thyroiditis and Grave's disease, represent complex conditions characterized by dysregulation of the immune system targeting the thyroid gland. Understanding the molecular and immunological mechanisms underlying the transition from Hashimoto's thyroiditis to Grave's disease is essential for unraveling the pathophysiology of these interconnected autoimmune conditions. We propose insights into the intricate interplay of genetic factors, immune responses, and hormonal pathways that drive the progression from hypothyroidism to hyperthyroidism, shedding light on new perspectives for diagnosis, management, and future research directions in autoimmune thyroid disorders. [ABSTRACT FROM AUTHOR]

The pentameric γ-Aminobutyric acid type A receptors (GABAARs) are ligand-gated ion channels that mediate the majority of inhibitory neurotransmission in the brain. In the cerebellum, the two main receptor subtypes are the 2α1/2β/γ and 2α6/2β/δ subunits. In the present study, an interaction proteomics workflow was used to reveal additional subtypes that contain both α1 and α6 subunits. Immunoprecipitation of the α6 subunit from mouse brain cerebellar extract co-purified the α1 subunit. In line with this, pre-incubation of the cerebellar extract with anti-α6 antibodies and analysis by blue native gel electrophoresis mass-shifted part of the α1 complexes, indicative of the existence of an α1α6-containing receptor. Subsequent mass spectrometry of the blue native gel showed the α1α6-containing receptor subtype to exist in two main forms, i.e., with or without Neuroligin-2. Immunocytochemistry on a cerebellar granule cell culture revealed co-localization of α6 and α1 in post-synaptic puncta that apposed the presynaptic marker protein Vesicular GABA transporter, indicative of the presence of this synaptic GABAAR subtype. [ABSTRACT FROM AUTHOR]