Anti-Dsk2 抗体 (ab4119)

Dsk2p is a member of a protein family that is characterized by possession of an N-terminal ubiquitin (Ub)-like (UbL) domain and a C-terminal Ub-associated (UBA) domain. In yeast, DSK2 was isolated as a suppressor of kar1, which is defective in spindle pole duplication. Although DSK2 is not an essential gene, yeast strains deleted for both DSK2 and RAD23 are temperature-sensitive for growth because of a block of spindle pole body duplication. Dsk2p and Rad23p seems to perform overlapping functions, although the sequence of Dsk2p is hardly similar to that of Rad23p overall except that they show 30% identity in their N-terminal UbL domains (residues 1-76) and that both contain UBA domains at their C terminus. Recent work on yeast Rad23p indicates that it is connected with the Ub-proteasome pathway; the N-terminal UbL domain interacts with the proteasome. There are genetic interactions between RAD23 and the polyubiquitin-binding subunit of the proteasome, RPN10, and Rad23p seems to inhibit polyubiquitin chain assembly in a cell-free assay system. It has recently been identified that Xenopus Dsk2-related protein, XDRP1, blocked Ub-dependent degradation of the cyclin A, and the human homologue of XDRP1, Plic1, is reported to form a link between the Ub machinery and the proteasome. Plic1 also is known as ubiquilin, independently isolated in a yeast two-hybrid screen by using presenilin as bait.

Nuclear