USP14

USP14

A gene on chromosome 18p11.32 that encodes a deubiquitinase which releases ubiquitin from the proteasome-targeted ubiquitinated proteins, ensuring that ubiquitin is regenerated at the proteasome. USP14 is required for the degradation of the chemokine receptor CXCR4, which is critical for CXCL12-induced cell chemotaxis, and serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) by inhibiting the degradation of unfolded ER proteins via interaction with ERN1. USP14 is required for synaptic development and function at neuromuscular junctions.
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Additionally, Rpn1 interacts with the ubiquitin-like domain, enabling the recruitment of shuttle factors such as human DNA repair protein (hHR23) and deubiquitinating enzyme (ubiquitin-specific protease 14; Usp14).
Family Members USPL1, CYLD, USP1, USP2, USP3, USP4, USP5, USP6, USP7, USP YSP8, USP9x, USP10, USP11, USP12, USP13, USP14, USP15, USP16, USP17L2, USP18, USP19, USP20, USP21, USP22, USP23, USP24, USP25, USP26, USP27, USP28, USP29, USP30, USP31, USP32, USP33, USP34, USP35, USP36, USP37, USP38, USP39, USP40, USP41, USP42, USP43, USP44, USP45, USP46, USP47, USP48, USP49, USP50, USP51, USP52, USP53, USP54 OTUB1, OTUB2, OTUD1, OTUD3, OTUD4, OTUD5, OTUD6A, OTU OTUD6B, OTU1, HIN1L, A20, Cezanne, Cezanne2, TRABID, VCPIP1 UCH UCH-L1, UCH-L3, UCH37/UCH-L5, BAP1 Josephin ATXN3, ATXN3L, JOSD1, JOSD2 JAMM/MPN+ BRCC36, CSNS, POH1, AMSH, AMSH-LP, MPND, MYSM1, PRPF8 Table 2: Deubiquitinases and bone remodeling.
It was reported yesterday that the collaboration is aimed at researching and developing new therapies based on the inhibition of Usp14, a deubiquitinating enzyme, for the treatment of certain neurodegenerative disorders.
San Diego, CA, November 24, 2013 --(PR.com)-- Markus Haeberlein, Senior Vice President and Head of Research at Proteostasis Therapeutics will give a presentation titled “The Development of Usp14 Inhibition as Disease-Modification, Therapeutics for Protein Aggregation Diseases,” at the 4th Ubiquitin Research and Drug Discovery Conference to be held in San Diego, CA on February 20-21, 2014 by GTC.
To better understand just what causes this malfunction, a research team led by Harvard Medical School researchers Daniel Finley, professor of cell biology, and Randall King, associate professor of cell biology, zeroed in on an enzyme called Usp14.
They found that, when activated, Usp14 disassembles the ubiquitin chain, slowing down the proteasome's ability to rid the cell of bad proteins.
The researchers wanted to see if they could find a molecule that inhibited Usp14, thus allowing the proteosome to work effectively.
Lee screened 63,000 compounds, looking for molecules that inhibited only Usp14 and could easily infiltrate the cell.
Experimenting in both human and mouse cell cultures, Min Jae Lee, also a postdoctoral researcher, and his co-workers found that IU1 inhibited Usp14 and allowed the proteasome to dispose of proteins more quickly.