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3  structures 595  species 0  interactions 633  sequences 6  architectures

Family: Cut8 (PF08559)

Summary: Cut8, nuclear proteasome tether protein

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Cut8, nuclear proteasome tether protein Provide feedback

In Schizosaccharomyces pombe, Cut8 is a nuclear envelope protein that physically interacts with and tethers 26S proteasome in the nucleus resulting in the nuclear accumulation of proteasome [1]. Cut8 comprises three functional domains. An N-terminal lysine-rich segment which binds to the proteasome when ubiquitinated, a central dimerisation domain and a C-terminal nine-helix, 3q5w bundle which shows structural similarity to 14-3-3 phosphoprotein-binding domains. The helical bundle is necessary for liposome and cholesterol binding [2]. Cut8 is a proteasome substrate and the N-terminal segment is polyubiquitinated and functions as a degron tag. Ubiquitination of the amino N-terminal segment is essential for the function of Cut8 [1]. Lysine residues in the N-terminal segment of Cut8 are required for physical interaction with proteasome [1]. In fission yeast the function of Cut8 has been demonstrated to be regulated by ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1 [1]. Cut8 homologues have been identified in Drosophila melanogaster, Anopheles gambiae and Dictyostelium discoideum [1].

Literature references

  1. Takeda K, Yanagida M; , Cell 2005;122:393-405.: Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8. PUBMED:16096059 EPMC:16096059

  2. Takeda K, Tonthat NK, Glover T, Xu W, Koonin EV, Yanagida M, Schumacher MA;, Proc Natl Acad Sci U S A. 2011;108:16950-16955.: Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8. PUBMED:21976488 EPMC:21976488


This tab holds annotation information from the InterPro database.

InterPro entry IPR013868

This entry includes fission yeast Cut8 protein and its homologue, Sts1.

In Schizosaccharomyces pombe, Cut8 is a nuclear envelope protein that physically interacts with and tethers 26S proteasome in the nucleus resulting in the nuclear accumulation of proteasome [PUBMED:16096059]. Cut8 comprises three functional domains. An N-terminal lysine-rich segment which binds to the proteasome when ubiquitinated, a central dimerisation domain and a C-terminal nine-helix, , bundle which shows structural similarity to 14-3-3 phosphoprotein-binding domains. The helical bundle is necessary for liposome and cholesterol binding [PUBMED:21976488]. Cut8 is a proteasome substrate and the N-terminal segment is polyubiquiti