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Gene Review

SEC66  -  Sec66p

Saccharomyces cerevisiae S288c

Synonyms: HSS1, Protein HSS1, SEC71, Sec62/63 complex 31.5 kDa subunit, Translocation protein SEC66, ...
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High impact information on SEC66

  • We demonstrate that Sec62p, Sec71p and Sec72p form a translocon subcomplex that engages secretory precursors at the membrane site of the ER translocation machinery [1].
  • Similar COP1-binding motifs containing an essential aromatic residue were identified in the cytoplasmic domain of an ER-resident protein, Sec71p, and in an ER retention motif previously characterized in the CD3epsilon chain of the T-cell receptor [2].
  • Taken together, these results suggest a direct role for Sec63p, Sec71p, and Sec72p in nuclear membrane fusion and argue against the alternative interpretation that the karyogamy defects result as an indirect consequence of the impaired membrane translocation of another component(s) required for the process [3].
  • Disruption of the genes encoding other Sec63p-associated proteins (Sec71p and Sec72p) also results in karyogamy defects [3].
  • We demonstrate here that the transmembrane domain (TMD) of Sec71p, a type-III membrane protein, contains an ER localization signal, which is required for physical recognition by Rer1p [4].

Biological context of SEC66


Associations of SEC66 with chemical compounds


Other interactions of SEC66

  • Moreover, in sec71 mutants, Kar5p was absent from the SPB and was not detected by Western blot or immunoprecipitation of pulse-labeled protein [5].
  • The mutants were contained in three complementation groups, which we have named SEC70, SEC71, and SEC72 [8].
  • Intracellular fluorescence images for Mid1 were the same as those for the ER marker protein Sec71 but quite different from those of the Golgi protein Ypt1 [9].
  • In the work on yeast Saccharomyces cerevisiae, we have demonstrated that transmembrane domains of a subset of ER membrane proteins including Sec12p, Sec71p and Sec63p contain novel ER retrieval signals [10].


  1. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Lyman, S.K., Schekman, R. Cell (1997) [Pubmed]
  2. New COP1-binding motifs involved in ER retrieval. Cosson, P., Lefkir, Y., Démollière, C., Letourneur, F. EMBO J. (1998) [Pubmed]
  3. ER membrane protein complex required for nuclear fusion. Ng, D.T., Walter, P. J. Cell Biol. (1996) [Pubmed]
  4. Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Sato, K., Sato, M., Nakano, A. Mol. Biol. Cell (2003) [Pubmed]
  5. Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae. Brizzio, V., Khalfan, W., Huddler, D., Beh, C.T., Andersen, S.S., Latterich, M., Rose, M.D. Mol. Biol. Cell (1999) [Pubmed]
  6. Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum. Feldheim, D., Yoshimura, K., Admon, A., Schekman, R. Mol. Biol. Cell (1993) [Pubmed]
  7. Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus. Kurihara, T., Silver, P. Mol. Biol. Cell (1993) [Pubmed]
  8. Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. Green, N., Fang, H., Walter, P. J. Cell Biol. (1992) [Pubmed]
  9. Subcellular localization and oligomeric structure of the yeast putative stretch-activated Ca2+ channel component Mid1. Yoshimura, H., Tada, T., Iida, H. Exp. Cell Res. (2004) [Pubmed]
  10. The Arabidopsis thaliana RER1 gene family: its potential role in the endoplasmic reticulum localization of membrane proteins. Sato, K., Ueda, T., Nakano, A. Plant Mol. Biol. (1999) [Pubmed]
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