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Gene Review

UBX2  -  Ubx2p

Saccharomyces cerevisiae S288c

Synonyms: SEL1, Secretion lowering protein 1, UBX domain-containing protein 2, YM9571.05, YML013W
 
 
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High impact information on SEL1

  • Two new papers reveal that the Ubx2 protein physically links ER-membrane-integrated ubiquitin ligases to Cdc48p, and that it is essential for degradation of substrates that are ubiquitylated at the cytoplasmic face of the ER [1].
  • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation [2].
  • Here we show that the UBX domain protein Ubx2 is an integral ER membrane protein that recruits Cdc48 to the ER [2].
  • Structure, function, and expression of SEL-1, a negative regulator of LIN-12 and GLP-1 in C. elegans [3].
  • The two major yeast UBX domain proteins, Shp1 and Ubx2, possess a ubiquitin-binding UBA domain and interact with ubiquitylated proteins in vivo [4].
 

Biological context of SEL1

  • SEL1 isolated from S. cerevisiae suppressed the super-secretion phenotype in K. lactis klsel1 strain, likewise homologous KlSEL1 [5].
  • These results suggest that HRD1 and SEL1 are up-regulated by the UPR and contribute to protection against the ER stress-induced cell death by degrading unfolded proteins accumulated in the ER [6].
 

Physical interactions of SEL1

  • The membrane protein Ubx2 contains a UBX domain that interacts with Cdc48 and an additional UBA domain [7].
 

Other interactions of SEL1

  • Ubx2 links the Cdc48 complex to ER-associated protein degradation [7].
  • Thus, a complex comprising the AAA ATPase, a ubiquitin ligase and the recruitment factor Ubx2 has a central role in ER-associated proteolysis [7].

References

  1. Cdc48p is UBX-linked to ER ubiquitin ligases. Römisch, K. Trends Biochem. Sci. (2006) [Pubmed]
  2. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Schuberth, C., Buchberger, A. Nat. Cell Biol. (2005) [Pubmed]
  3. Structure, function, and expression of SEL-1, a negative regulator of LIN-12 and GLP-1 in C. elegans. Grant, B., Greenwald, I. Development (1997) [Pubmed]
  4. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. Schuberth, C., Richly, H., Rumpf, S., Buchberger, A. EMBO Rep. (2004) [Pubmed]
  5. Studies of yeast Kluyveromyces lactis mutations conferring super-secretion of recombinant proteins. Bartkeviciute, D., Sasnauskas, K. Yeast (2003) [Pubmed]
  6. ER signaling in unfolded protein response. Kaneko, M., Nomura, Y. Life Sci. (2003) [Pubmed]
  7. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Neuber, O., Jarosch, E., Volkwein, C., Walter, J., Sommer, T. Nat. Cell Biol. (2005) [Pubmed]
 
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