title: Role for the neurexin-neuroligin complex in Alzheimer's disease.
abstract: Synaptic damage is a critical hallmark of Alzheimer's disease, and the best correlate with cognitive impairment ante mortem. Synapses, the loci of communication between neurons, are characterized by signature protein combinations arrayed at tightly apposed pre- and post-synaptic sites. The most widely studied trans-synaptic junctional complexes, which direct synaptogenesis and foster the maintenance and stability of the mature terminal, are conjunctions of presynaptic neurexins and postsynaptic neuroligins. Fluctuations in the levels of neuroligins and neurexins can sway the balance between excitatory and inhibitory neurotransmission in the brain, and could lead to damage of synapses and dendrites. This review summarizes current understanding of the roles of neurexins and neuroligins proteolytic processing in synaptic plasticity in the human brain, and outlines their possible roles in β-amyloid metabolism and function, which are central pathogenic events in Alzheimer's disease progression.
authors.affiliation: Centre for Psychiatry and Clinical Neuroscience, School of Medicine, The University of Queensland, Brisbane, Australia.
authors.forename: Ikhlas A
authors.initials: IA
authors.lastname: Sindi
authors.affiliation: Centre for Psychiatry and Clinical Neuroscience, School of Medicine, The University of Queensland, Brisbane, Australia; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia.
authors.forename: Rudolph K
authors.initials: RK
authors.lastname: Tannenberg
authors.affiliation: School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia. Electronic address: uqpdodd@uq.edu.au.
authors.forename: Peter R
authors.initials: PR
authors.lastname: Dodd
mesh_terms: D000110:Acetylcholinesterase / Q000502:physiology; D017398:Alternative Splicing / Q000502:physiology; D000544:Alzheimer Disease / Q000235:genetics* / Q000378:metabolism* / Q000473:pathology / Q000523:psychology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D001921:Brain / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D002135:Calcium-Binding Proteins; D015816:Cell Adhesion Molecules, Neuronal; D002450:Cell Communication / Q000235:genetics / Q000502:physiology; D018450:Disease Progression; D006801:Humans; D007858:Learning; D008568:Memory; D009419:Nerve Tissue Proteins; D019006:Neural Cell Adhesion Molecules / Q000502:physiology*; D009473:Neuronal Plasticity / Q000235:genetics / Q000502:physiology; D009474:Neurons / Q000473:pathology / Q000502:physiology; D013569:Synapses / Q000235:genetics* / Q000473:pathology / Q000502:physiology
chemical_list: D016229:Amyloid beta-Peptides; D002135:Calcium-Binding Proteins; D015816:Cell Adhesion Molecules, Neuronal; C539628:NRXN1 protein, human; D009419:Nerve Tissue Proteins; D019006:Neural Cell Adhesion Molecules; C093438:neuroligin 1; D000110:Acetylcholinesterase
keywords: Alternative splicing; Cell adhesion molecules; Excitatory synapses; Inhibitory synapses; Neurodegeneration; acetylcholinesterase (AChE)