High impact information on DSK2

• Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins such as Rad23 and Dsk2 mediate the delivery of polyubiquitinated proteins to the proteasome in the ubiquitin-proteasome pathway [1].
• Dsk2p is a nuclear-enriched protein, and we propose that Dsk2p assists in Cdc31 assembly into the new SPB [2].
• Suppressors of a kar1 allele defective for SPB duplication were isolated in two genes, CDC31 and DSK2 (Vallen, E.A., W.H., M. Winey, and M.D. Rose. 1994. Genetics. 137:407-422) [2].
• Therefore, DSK2 does not act by interfering with ubiquitin-dependent protein degradation of these proteins [2].
• Unlike ubiquitin, the NH2-terminal domain of Dsk2p is not cleaved from the protein, indicating that Dsk2p is not conjugated to other proteins [2].

Biological context of DSK2

• Eleven extragenic suppressor mutations mapped to two linkage groups, DSK1 and DSK2 [3].
• Rad23 and Dsk2 dimerization requires their UBL and/or UBA domains whereas Ddi1 dimerization does not [4].

Associations of DSK2 with chemical compounds

• To elucidate the role of DSK2 in SPB duplication, we cloned the gene and found it encodes a novel ubiquitin-like protein containing an NH2 terminus 36% identical to ubiquitin [2].

Physical interactions of DSK2

• Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition [5].

Other interactions of DSK2

• Although DSK2 is not essential, a strain deleted for both DSK2 and RAD23 is temperature sensitive for growth due to a block in SPB duplication [2].

References