DSK2 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.
Bowman S, Churcher C, Badcock K, Brown D, Chillingworth T, Connor R, Dedman K, Devlin K, Gentles S, Hamlin N, Hunt S, Jagels K, Lye G, Moule S, Odell C, Pearson D, Rajandream M, Rice P, Skelton J, Walsh S, Whitehead S, Barrell B
Nature387(6632 Suppl)90-3(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Proteasome/autophagy pathway choice is independent of the ubiquitin-binding properties of the receptors Dsk2/Cue5 but largely determined by their oligomerization potentials.
Title: Receptor oligomerization guides pathway choice between proteasomal and autophagic degradation.

Identify the Cdc48-Rad23/Dsk2 axis as a major route to the proteasome.
Title: In?Vivo Ubiquitin Linkage-type Analysis Reveals that the Cdc48-Rad23/Dsk2 Axis Contributes to K48-Linked Chain Specificity of the Proteasome.

functional yeast proteasomes have the capacity to associate and dissociate with Rpn10 and that Rpn10 monoubiquitination decreases the Rpn10-proteasome and Rpn10-Dsk2 associations.
Title: Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome.

These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.
Title: Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast.

C-terminal UBA domain of Dsk2 ubiquitin receptor protects it by preventing initiation of protein degradation at the proteasome.
Title: C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation.