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Subcellular organization of UBE3A in neurons.

ABSTRACT: Ubiquitination regulates a broad array of cellular processes, and defective ubiquitination is implicated in several neurological disorders. Loss of the E3 ubiquitin-protein ligase UBE3A causes Angelman syndrome. Despite its clinical importance, the normal role of UBE3A in neurons is still unclear. As a step toward deciphering its possible functions, we performed high-resolution light and electron microscopic immunocytochemistry. We report a broad distribution of UBE3A in neurons, highlighted by concentrations in axon terminals and euchromatin-rich nuclear domains. Our findings suggest that UBE3A may act locally to regulate individual synapses while also mediating global, neuronwide influences through the regulation of gene transcription. J. Comp. Neurol. 525:233-251, 2017. © 2016 Wiley Periodicals, Inc.

SUBMITTER: Burette AC

PROVIDER: S-EPMC5138109 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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Subcellular organization of UBE3A in neurons.

Burette Alain C AC Judson Matthew C MC Burette Susan S Phend Kristen D KD Philpot Benjamin D BD Weinberg Richard J RJ

The Journal of comparative neurology 20160711 2

Ubiquitination regulates a broad array of cellular processes, and defective ubiquitination is implicated in several neurological disorders. Loss of the E3 ubiquitin-protein ligase UBE3A causes Angelman syndrome. Despite its clinical importance, the normal role of UBE3A in neurons is still unclear. As a step toward deciphering its possible functions, we performed high-resolution light and electron microscopic immunocytochemistry. We report a broad distribution of UBE3A in neurons, highlighted by ...[more]

PMID: 27339004

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Subcellular organization of UBE3A in human cerebral cortex.

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Corrigendum: Angelman syndrome-derived neurons display late onset of paternal UBE3A silencing.

Project description:This corrects the article DOI: 10.1038/srep30792.

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A bipartite boundary element restricts <i>UBE3A</i> imprinting to mature neurons.

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