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Deubiquitination of EPG5 by USP8 guards the autophagic flux in embryonic stem cells (ESCs) to maintain their stemness. This work uncovers a novel crosstalk pathway between ubiquitination and autophagy through USP8-EPG5 interaction to regulate the stemness of ESCs.
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USP8 interacted with transforming growth factorbetaactivated kinase1 (TAK1) and deubiquitinated the K63linked ubiquitination of TAK1.
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UBPy-sorted cargo to acrosome biogenesis and effects of its derailment in a mouse model of globozoospermia, the infertile Vps54 (L967Q) mutant, are reported.
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the membrane receptor MET, described herein for the first time in spermatids, is a USP8/UBPy-target substrate is delivered to the acrosome.
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in neuronal cells USP8 could be involved in endosomal trafficking, retrograde transport and synaptic plasticity. In disorders leading to neurodegeneration USP8 is upregulated and could influence the neuron-oligodendrocyte interactions.
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The spatio-temporal expression of mUBPy suggests that the enzyme may be involved in neuroregulatory processes during embryogenesis.
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a role for the USP8.STAM complex as a protective mechanism regulating early endosomal sorting of EGFR between pathways destined for lysosomal degradation and recycling.
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USP8 was able to interact with spermatid endosomal-sorting complex required for transport-0 and microtubule structures; USP8 can directly link, via its MIT domain, the labeled vesicles/developing acrosome to microtubules.
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in wobbler testis expression of mouse ubiquitin-specific processing protease (mUBPy)is up-regulated, while a differential sorting of the protein characterizes wobbler spermatids where acrosome formation is impaired
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Data indicate a novel mechanism where diacylglycerol kinase delta and protein kinase Calpha modulate the levels of ubiquitinated epidermal growth factor receptors through Akt and ubiquitin-specific protease 8.
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deubiquitinating enzyme specifically expressed in testis, associates with the acrosome and centrosome in mouse germ cells
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Results indicate that Nrdp1 is a specific target for the USP8 deubiquitinating enzyme and are consistent with a model where USP8 augments Nrdp1 activity by mediating its stabilization.
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We conclude that UBPY negatively regulates the rate of EGFR down-regulation by deubiquitinating EGFR on endosomes.
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UBPY-mediated EGFR de-ubiquitination promotes EGFR degradation
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UBPy may play a key role during mouse fertilization as a novel centrosomal component.
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These results unveil a central and nonredundant role of UBPy in growth regulation, endosomal sorting, and the control of receptor tyrosine kinases in vivo.
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UBPY is catalytically inhibited in a phosphorylation-dependent manner by 14-3-3s during the interphase, and this regulation is cancelled in the M phase.
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Moderate expression of mouse UBPy was found in the amygdaloid complex, supraoptic nucleus, arcuate and ventromedial nuclei of hypothalamus, lateral hypothalamic area and lateral and reticular part of the substantia nigra.