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UFD1  -  polyubiquitin-binding protein UFD1

Saccharomyces cerevisiae S288c

Synonyms: PIP3, Polymerase-interacting protein 3, UB fusion protein 1, Ubiquitin fusion degradation protein 1, YGR048W
 
 
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High impact information on UFD1

  • Therefore, Cdc48/p97-Ufd1-Npl4 is an essential chaperone that regulates transformation of the microtubule structure as cells reenter interphase [1].
  • In the absence of p97-Ufd1-Npl4 function, microtubules in Xenopus egg extracts remain as monopolar spindles attached to condensed chromosomes after Cdc2 kinase activity has returned to the interphase level [1].
  • PIP2 and PIP3: complex roles at the cell surface [2].
  • Formation of a closed NE requires the p97-Ufd1-Npl4 complex, not previously implicated in membrane fusion [3].
  • Here, we have studied the mechanism by which the p97-Ufd1-Npl4 complex functions in this retrotranslocation pathway [4].
 

Biological context of UFD1

  • Here, we present the solution structure of yeast Ufd1 N domain and show that it has two distinct binding sites for mono- and polyubiquitin [5].
  • Here, we discuss the possibility that the Cdc48/ p97-Ufd1-Npl4 complex has a more general role in mediating morphological transitions as the cell exits mitosis and enters G(1) [6].
  • With the noninvestigated exception of haptophytes a phylogenetically and mechanistically related system is apparently present in all chromalveolates with 4 membrane-bound plastids because amongst others, PPC-specific Derlins (Der1-like proteins), CDC48 and its cofactor Ufd1 were identified in the nuclear genomes of diatoms and apicomplexa [7].
  • The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts [8].
  • A S. pombe mutant containing a frameshift mutation at the beginning of the carboxy-terminal half of gene ufd1 (the Saccharomyces cerevisiae UFD1 homologue) is cordycepin-resistant and sterile [9].
 

Anatomical context of UFD1

  • The only functional data available about mammalian Ufd1p is the ability to form a complex with the rat Npl4 protein, a component of the nuclear pore complex [10].
  • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains [4].
  • The AAA ATPase Cdc48/p97 together with its adaptors, Ufd1-Npl4, regulate membrane-related functions and mitotic spindle disassembly by directly binding to membrane-associated proteins or spindle assembly factors, modulating their interactions with membranes or spindles, respectively [6].
  • Valosin-containing Protein (p97) Is a Regulator of Endoplasmic Reticulum Stress and of the Degradation of N-End Rule and Ubiquitin-Fusion Degradation Pathway Substrates in Mammalian Cells [11].
 

Associations of UFD1 with chemical compounds

  • Polyubiquitin chains linked by lysine 48 are recognized in a synergistic manner by both p97 and an evolutionarily conserved ubiquitin-binding site at the NH2 terminus of Ufd1 [4].
 

Physical interactions of UFD1

  • Neither cytosolic chaperones nor Cdc48p/Ufd1p/Npl4p complex components or proteasome activity are required for ER exit, indicating that K28 retrotranslocation is mechanistically different from classical ER-associated protein degradation (ERAD) [12].
  • Both Uba2 and Ufd1 can be co-immunoprecipitated from extracts with Pap1, confirming in vitro the interaction identified by two-hybrid analysis [8].
 

Other interactions of UFD1

  • We also found that each member of the Cdc48p-Ufd1p-Npl4p complex is individually required for ERAD [13].
  • We show that these two proteins are probably delivery factors for ubiquitinated ER substrates to the proteasome, following their removal from the membrane via the Cdc48-Ufd1-Npl4p complex [14].
  • Two of the five genes thus identified, UFD1 and UFD5, function at post-ubiquitination steps in the UFD pathway [15].
  • The Ufd1-ubiquitin interaction is essential for transfer of substrates to the proteasome [5].
  • To determine the property of Ufd2, we reconstituted the UFD pathway using purified enzymes from yeast [16].

References

  1. The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cao, K., Nakajima, R., Meyer, H.H., Zheng, Y. Cell (2003) [Pubmed]
  2. PIP2 and PIP3: complex roles at the cell surface. Czech, M.P. Cell (2000) [Pubmed]
  3. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Hetzer, M., Meyer, H.H., Walther, T.C., Bilbao-Cortes, D., Warren, G., Mattaj, I.W. Nat. Cell Biol. (2001) [Pubmed]
  4. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. Ye, Y., Meyer, H.H., Rapoport, T.A. J. Cell Biol. (2003) [Pubmed]
  5. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Park, S., Isaacson, R., Kim, H.T., Silver, P.A., Wagner, G. Structure (Camb.) (2005) [Pubmed]
  6. The Cdc48/p97-Ufd1-Npl4 complex: its potential role in coordinating cellular morphogenesis during the M-G1 transition. Cao, K., Zheng, Y. Cell Cycle (2004) [Pubmed]
  7. Der1-mediated Preprotein Import into the Periplastid Compartment of Chromalveolates? Sommer, M.S., Gould, S.B., Lehmann, P., Gruber, A., Przyborski, J.M., Maier, U.G. Mol. Biol. Evol. (2007) [Pubmed]
  8. The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts. del Olmo, M., Mizrahi, N., Gross, S., Moore, C.L. Mol. Gen. Genet. (1997) [Pubmed]
  9. Cordycepin in Schizosaccharomyces pombe: effects on the wild type and phenotypes of mutants resistant to the drug. Naula, N., Hilti, N., Schweingruber, A.M., Schweingruber, M.E. Curr. Genet. (2003) [Pubmed]
  10. Cloning and characterization of the gene encoding human NPL4, a protein interacting with the ubiquitin fusion-degradation protein (UFD1L). Botta, A., Tandoi, C., Fini, G., Calabrese, G., Dallapiccola, B., Novelli, G. Gene (2001) [Pubmed]
  11. Valosin-containing Protein (p97) Is a Regulator of Endoplasmic Reticulum Stress and of the Degradation of N-End Rule and Ubiquitin-Fusion Degradation Pathway Substrates in Mammalian Cells. W??jcik, C., Rowicka, M., Kudlicki, A., Nowis, D., McConnell, E., Kujawa, M., Demartino, G.N. Mol. Biol. Cell (2006) [Pubmed]
  12. Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. Heiligenstein, S., Eisfeld, K., Sendzik, T., Jimen??z-Becker, N., Breinig, F., Schmitt, M.J. EMBO J. (2006) [Pubmed]
  13. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Bays, N.W., Wilhovsky, S.K., Goradia, A., Hodgkiss-Harlow, K., Hampton, R.Y. Mol. Biol. Cell (2001) [Pubmed]
  14. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. Medicherla, B., Kostova, Z., Schaefer, A., Wolf, D.H. EMBO Rep. (2004) [Pubmed]
  15. A proteolytic pathway that recognizes ubiquitin as a degradation signal. Johnson, E.S., Ma, P.C., Ota, I.M., Varshavsky, A. J. Biol. Chem. (1995) [Pubmed]
  16. Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage. Saeki, Y., Tayama, Y., Toh-e, A., Yokosawa, H. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
 
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