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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Ubiquitin specific peptidase 33

VDU1, USP33
Top mentioned proteins: Ubiquitin, VDU2, CAN, V1a, VHL
Papers on VDU1
Specific CP110 Phosphorylation Sites Mediate Anaphase Catastrophe after CDK2 Inhibition: Evidence for Cooperation with USP33 Knockdown.
New
Dmitrovsky et al., United States. In Mol Cancer Ther, Nov 2015
Finally, CDK2 inhibitor response was enhanced when combined with knockdown of the deubiquitinase USP33 that in turn accelerates CP110 protein degradation.
USP33 mediates Slit-Robo signaling in inhibiting colorectal cancer cell migration.
New
Wu et al., Wuxi, China. In Int J Cancer, May 2015
Robo-interacting ubiquitin-specific protease 33 (USP33) is required for the inhibitory function of Slit2 on CRC cell migration by deubiquitinating and stabilizing Robo1.
Phosphorylation of the deubiquitinase USP20 by protein kinase A regulates post-endocytic trafficking of β2 adrenergic receptors to autophagosomes during physiological stress.
New
Shenoy et al., Durham, United States. In J Biol Chem, May 2015
Ubiquitination by the E3 ligase Nedd4 and deubiquitination by the deubiquitinases USP20 and USP33 have been shown to regulate the lysosomal trafficking and recycling of agonist-activated β2 adrenergic receptors (β2ARs).
Regulation of neuronal morphogenesis and positioning by ubiquitin-specific proteases in the cerebellum.
Bonni et al., Saint Louis, United States. In Plos One, 2014
In RNAi screens of the 32 neuronally expressed USPs, we uncover novel functions for USP1, USP4, and USP20 in the morphogenesis of granule neuron dendrites and axons and we identify a requirement for USP30 and USP33 in granule neuron migration in the rodent cerebellar cortex in vivo.
USP33, a new player in lung cancer, mediates Slit-Robo signaling.
Wu et al., Beijing, China. In Protein Cell, 2014
Ubiquitin specific protease 33 (USP33) is a multifunctional protein regulating diverse cellular processes.
Degradation of the deubiquitinating enzyme USP33 is mediated by p97 and the ubiquitin ligase HERC2.
Chan et al., Pasadena, United States. In J Biol Chem, 2014
Because the deubiquitinating enzyme USP33 is involved in several important cellular processes (β-adrenergic receptor recycling, centrosome amplification, RalB signaling, and cancer cell migration), its levels must be carefully regulated.
The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response.
Impact
Sablina et al., Leuven, Belgium. In Nat Cell Biol, 2013
In contrast, nutrient starvation induces RALB deubiquitylation by accumulation and relocalization of the deubiquitylase USP33 to RALB-positive vesicles.
Cell biology: DUBing CP110 controls centrosome numbers.
Hoffmann et al., Heidelberg, Germany. In Curr Biol, 2013
A recent study reveals that the deubiquitinating enzyme USP33 regulates centrosome biogenesis by stabilizing the centriolar protein CP110.
USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110.
Impact
Dynlacht et al., New York City, United States. In Nature, 2013
Here, using human cells, we report a new mechanism for the regulation of centrosome duplication that requires USP33, a deubiquitinating enzyme that is able to regulate CP110 levels.
MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound β(2)-adrenergic receptors.
Shenoy et al., Durham, United States. In J Cell Biol, 2012
Carvedilol prevented β(2)AR recycling, blocked recruitment of Nedd4 E3 ligase, and promoted the dissociation of the deubiquitinases USP20 and USP33.
[A comparative biopharmaceutical study of brands of ciprofloxacin tablets available on the Colombian market].
Pájaro-Bolívar et al., Cartagena, Colombia. In Rev Salud Publica (bogota), 2012
CONCLUSIONS: 11 products complied with USP33-NF28specifications (guidelines on specifications for impurities in antibiotics).
Isoform-specific localization of the deubiquitinase USP33 to the Golgi apparatus.
Clague et al., Liverpool, United Kingdom. In Traffic, 2011
Ubiquitin-specific protease 33 (USP33) is a deubiquitinase that has been associated with a variety of physiological events.
Type 2 deiodinase at the crossroads of thyroid hormone action.
Review
Bianco et al., Miami, United States. In Int J Biochem Cell Biol, 2011
Inactivation involves disruption of the D2:D2 dimer and can be reversed via two ubiquitin-specific proteases, USP20 and USP33, rescuing catalytic activity and T3 production.
Midline crossing and Slit responsiveness of commissural axons require USP33.
GeneRIF
Wu et al., Chicago, United States. In Nat Neurosci, 2009
Our results reveal a previously unknown role for USP33 in vertebrate commissural axon guidance and in Slit signaling
Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration.
GeneRIF
Wu et al., Chicago, United States. In Proc Natl Acad Sci U S A, 2009
Data uncover a previously unknown function of USP33 and reveal a new player in Slit-Robo signaling in cancer cell migration.
The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization.
GeneRIF
Shenoy et al., Durham, United States. In Embo J, 2009
USPs 20 and 33 serve as novel regulators that dictate both post-endocytic sorting as well as the intensity and extent of beta(2)AR signalling from the cell surface.
Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.
GeneRIF
Lefkowitz et al., Durham, United States. In Proc Natl Acad Sci U S A, 2009
USP33 and Mdm2 function reciprocally and favor respectively the stability or lability of the receptor beta-arrestin complex
Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner.
GeneRIF
Sytkowski et al., Boston, United States. In Biochem Biophys Res Commun, 2009
VDU1 was identified as a protein partner of hSP56.
Cellular and structural biology of the deiodinases.
Review
Larsen et al., Boston, United States. In Thyroid, 2005
This is because D2 interacts with and is a substrate of the pVHL-interacting deubiquitinating enzymes (VDU1 and VDU2), and thus the ubiquitination-deubiquitination cycles regulates the supply of active thyroid hormone in D2-expressing cells.
Triplets! Unexpected structural similarity among the three enzymes that catalyze initiation and termination of thyroid hormone effects.
Review
Bianco, Boston, United States. In Arq Bras Endocrinol Metabol, 2004
In addition, D2 interacts with and is a substrate of the pVHL-interacting deubiquitinating enzymes (VDU1 and VDU2); thus deubiquitination regulates the supply of active thyroid hormone in D2-expressing cells.
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