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Gene Review

COP1  -  Cop1p

Saccharomyces cerevisiae S288c

Synonyms: Alpha-COP, Alpha-coat protein, Coatomer subunit alpha, D1578, RET1, ...
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High impact information on COP1

  • 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 [1].
  • For example, binding of COP1 to dilysine (KKXX) motifs induces specific retrieval of tagged proteins from the Golgi back to the endoplasmic reticulum (ER) [1].
  • Extensive mutagenesis of deltaL identified an aromatic residue as a critical determinant of the interaction with COP1 [1].
  • In sec28 Delta cells shifted to 37 degrees C, wild-type alpha-COP (Ret1p) levels diminish rapidly and cells accumulate p1 CPY; these defects can be suppressed by alpha-COP overproduction [2].
  • Hence, our data provide molecular support for the hypothesis that COP1 is a convergence point for upstream signaling pathways dedicated to individual photoreceptors [3].

Biological context of COP1

  • In addition, stably expressed COP1 binds to major vault protein (MVP) and translocated promoter region (Tpr) [4].
  • The study of nuclear localization of factors such as COP1 and KN1 is now leading to models for regulating nuclear transport as well as intercellular transport of transcription factors [5].
  • Nucleotide sequencing of SOO1 revealed that this gene is identical to the recently reported alpha-COP that is involved in the intracellular protein translocation from endoplasmic reticulum to Golgi and vice versa [6].
  • To further investigate SPA1 function in the phyA signaling pathway, we tested whether SPA1, like COP1, mediates changes in gene expression in response to light [3].

Anatomical context of COP1

  • Complementation analysis revealed that sec32-1 is an allele of BOS1, a gene implicated in vesicle targeting to the Golgi complex, and sec33-1 is an allele of RET1, a gene that encodes the alpha subunit of coatomer [7].

Associations of COP1 with chemical compounds

  • The COP1 protein contains a cysteine-rich zinc-binding RING finger motif found in diverse groups of regulatory proteins [8].

Other interactions of COP1

  • Constitutive photomorphogenic 1 (COP1), a protein composed of a RING finger, a coiled-coil domain and seven WD40 repeats, functions as an E3 ubiquitin ligase that targets key transcription factors for ubiquitination and degradation in both higher plants and mammalian cells [4].
  • Furthermore we have characterized three new alleles of ret1 and showed that Golgi localization of Emp47p was intact in cells with those mutant alleles [9].


  1. New COP1-binding motifs involved in ER retrieval. Cosson, P., Lefkir, Y., Démollière, C., Letourneur, F. EMBO J. (1998) [Pubmed]
  2. epsilon-COP is a structural component of coatomer that functions to stabilize alpha-COP. Duden, R., Kajikawa, L., Wuestehube, L., Schekman, R. EMBO J. (1998) [Pubmed]
  3. The phytochrome A-specific signaling intermediate SPA1 interacts directly with COP1, a constitutive repressor of light signaling in Arabidopsis. Hoecker, U., Quail, P.H. J. Biol. Chem. (2001) [Pubmed]
  4. Affinity purification reveals the association of WD40 protein constitutive photomorphogenic 1 with the hetero-oligomeric TCP-1 chaperonin complex in mammalian cells. Yi, C., Li, S., Wang, J., Wei, N., Deng, X.W. Int. J. Biochem. Cell Biol. (2006) [Pubmed]
  5. Switching of gene expression: analysis of the factors that spatially and temporally regulate plant gene expression. Meisel, L., Lam, E. Genet. Eng. (N.Y.) (1997) [Pubmed]
  6. Identification of a gene, SOO1, which complements osmo-sensitivity and defect in in vitro beta1,3-glucan synthase activity in Saccharomyces cerevisiae. Lee, D.W., Ahn, G.W., Kang, H.G., Park, H.M. Biochim. Biophys. Acta (1999) [Pubmed]
  7. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Wuestehube, L.J., Duden, R., Eun, A., Hamamoto, S., Korn, P., Ram, R., Schekman, R. Genetics (1996) [Pubmed]
  8. The RING finger motif of photomorphogenic repressor COP1 specifically interacts with the RING-H2 motif of a novel Arabidopsis protein. Torii, K.U., Stoop-Myer, C.D., Okamoto, H., Coleman, J.E., Matsui, M., Deng, X.W. J. Biol. Chem. (1999) [Pubmed]
  9. Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport. Schröder-Köhne, S., Letourneur, F., Riezman, H. J. Cell. Sci. (1998) [Pubmed]
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