Ubiquitin is a small protein that is attached to other proteins by the means of ubiquitin ligases. Dependent on the number of ubiquitin molecules that are added in a row and the nature of their linkage, proteins are either marked for degradation or altered in their activity, subcellular localization or protein-protein interaction.
Ubiquitination is reversible and the removal of ubiquitin is catalysed by deubiquitinating enzymes. The human genome contains 95 putative DUB genes, which can be broadly classified as cysteine proteases and metalloproteases. Not all 95 DUBs are predicted to be functional enzymes.
The ubiquitination pathway has been implicated in a number of genetic disorders and diseases including cancer and neurological diseases which result from the build-up of protein aggregates such as; Alzheimer’s disease, Parkinson’s disease and Huntingdon’s disease.
This collection has been generated in close collaboration with Prof. Steve Jackson (Gurdon Institute, Cambridge, United Kingdom).
Deubiquitination of FANCD2 by USP1 is impacted in a USP1 knockout cell lines.
Cells were washed with PBS, lysed in Frackelton buffer (10 mM Tris/HCl pH 7.5, 50 mM NaCl, 30 mM sodium pyrophosphate, 1 % Triton X-100, 50 mM NaF and protease inhibitors).
They were analyzed by SDS-PAGE and Western blotting using anti-FANCD2 (sc-20022 from Santa Cruz). HAP1 wild-type cells were compared to cells bearing a frameshift mutation in USP1.
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