IndraLab

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USP46 deubiquitinates GRIA. 9 / 9
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"USP46, which is known to be enriched at the neural synapse, may modulate brain function by deubiquitinating AMPAR."

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"Ubiquitin-specific protease 46 (USP46) deubiquitinates the glutamate receptors GLR-1 and AMPAR, resulting in increased surface levels of these receptors [149, 150]."

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"In AD brains and neurons incubated with Aβ, USP46 expression is downregulated, triggering ubiquitination, and clearance of AMPARs."

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"They discovered that K63-type ubiquitination affects AMPARs and that both in vivo and in vitro, USP46 can deubiquitinate AMPARs."

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"All of these findings point to a conserved mechanism in which USP46 deubiquitinates AMPARs at synapses to prevent their breakdown and to encourage their recycling to the cell surface, which in turn impacts synapse function."

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"Given the same type of deubiquitinating enzyme (USP46) is able to deubiquitinate AMPA receptors, and knockdown of USP46 elevated AMPA receptor ubiquitination and reduced AMPA receptor expression in hi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Endogenous USP46 suppresses AMPAR ubiquitination in neurons."

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"We found that USP46 suppressed AMPAR ubiquitination leading to an increase in receptor protein amount as well as in receptor synaptic localization."

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"USP46 over-expression leads to a reduction in AMPAR ubiquitination, whereas knockdown of USP46 by either siRNAs or shRNAs causes a significant increase in AMPAR ubiquitination."