COPZ1

Summary

Gene Symbol: COPZ1
Description: coatomer protein complex subunit zeta 1
Alias: CGI-120, COPZ, HSPC181, zeta-COP, zeta1-COP, coatomer subunit zeta-1, coatomer protein complex, subunit zeta, zeta-1 COP, zeta-1-coat protein
Species: human
Products:     COPZ1

Top Publications

  1. Schekman R, Orci L. Coat proteins and vesicle budding. Science. 1996;271:1526-33 pubmed
    ..Secretion, which has been viewed as a default pathway, may require sorting and packaging signals on transported molecules to ensure their rapid delivery to the cell surface...
  2. Novoa Aponte L, Ramirez D, ARGUELLO J. The interplay of the metallosensor CueR with two distinct CopZ chaperones defines copper homeostasis in Pseudomonas aeruginosa. J Biol Chem. 2019;294:4934-4945 pubmed publisher
    ..contains a Cu+-sensing transcriptional regulator, CueR, and two homologous metal chaperones, CopZ1 and CopZ2, forming a unique system for studying Cu+ homeostasis...
  3. Padilla Benavides T, George Thompson A, McEvoy M, ARGUELLO J. Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF. J Biol Chem. 2014;289:20492-501 pubmed publisher
    ..Cytosolic Cu(+) chaperones (CopZ) interact with a structural platform in Cu(+)-ATPases (CopA) and deliver copper into the ion permeation path...
  4. Cao L, Yang C, Zhang B, Lv K, Li M, Deng K. Synergistic photocatalytic performance of cobalt tetra(2-hydroxymethyl-1,4-dithiin)porphyrazine loaded on zinc oxide nanoparticles. J Hazard Mater. 2018;359:388-395 pubmed publisher
    A new ZnO/CoPz(hmdtn)4 composite as a highly efficient photocatalyst was successfully prepared by cobalt tetra(2-hydroxymethyl-1,4-dithiin)porphyrazine (CoPz(hmdtn)4) impregnated onto the surface of ZnO nanoparticles,..
  5. Chaplin A, Tan B, Vijgenboom E, Worrall J. Copper trafficking in the CsoR regulon of Streptomyces lividans. Metallomics. 2015;7:145-55 pubmed publisher
    ..to apo-CsoR resulting in the transcriptional derepression of genes encoding for copper efflux systems involving CopZ-like copper chaperones and CopA-like P-type ATPases...
  6. Kay K, Zhou L, Tenori L, Bradley J, Singleton C, Kihlken M, et al. Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation. Chem Commun (Camb). 2017;53:1397-1400 pubmed publisher
    ..Here we report studies of copper transfer between the Atx1-type chaperone CopZ from Bacillus subtilis and the soluble domains of its cognate P-type ATPase transporter, CopAab...
  7. Young C, Gordon L, Fang Z, Holder R, Reid S. Copper Tolerance and Characterization of a Copper-Responsive Operon, copYAZ, in an M1T1 Clinical Strain of Streptococcus pyogenes. J Bacteriol. 2015;197:2580-92 pubmed publisher
    ..We defined a set of putative genes, copY (for a regulator), copA (for a P1-type ATPase), and copZ (for a copper chaperone), whose expression is regulated by copper...
  8. Singh K, Senadheera D, Lévesque C, Cvitkovitch D. The copYAZ Operon Functions in Copper Efflux, Biofilm Formation, Genetic Transformation, and Stress Tolerance in Streptococcus mutans. J Bacteriol. 2015;197:2545-57 pubmed publisher
    ..operon for copper homeostasis, where copA and copB encode copper-transporting P-type ATPases, whereas copY and copZ regulate the expression of the cop operon...
  9. Bensellam M, Maxwell E, Chan J, Luzuriaga J, West P, Jonas J, et al. Hypoxia reduces ER-to-Golgi protein trafficking and increases cell death by inhibiting the adaptive unfolded protein response in mouse beta cells. Diabetologia. 2016;59:1492-1502 pubmed publisher
    ..Coatomer protein complex genes (Copa, Cope, Copg [also known as Copg1], Copz1 and Copz2) and ER-to-Golgi protein trafficking were also reduced, whereas apoptotic genes (Ddit3, Atf3 and Trb3 [..

More Information

Publications34

  1. Anania M, Gasparri F, Cetti E, Fraietta I, Todoerti K, Miranda C, et al. Identification of thyroid tumor cell vulnerabilities through a siRNA-based functional screening. Oncotarget. 2015;6:34629-48 pubmed publisher
    ..Further analysis of three selected hit genes, namely Cyclin D1, MASTL and COPZ1, showed that they represent common vulnerabilities for thyroid tumor cells, as their inhibition reduced the ..
  2. Fu Y, Bruce K, Wu H, Giedroc D. The S2 Cu(i) site in CupA from Streptococcus pneumoniae is required for cellular copper resistance. Metallomics. 2016;8:61-70 pubmed publisher
    ..In contrast, the S2 site is essential for Cu resistance. Expression of a chimeric CopZ chaperone fused to the CupA transmembrane helix does not protect S...
  3. Straw M, Chaplin A, Hough M, Paps J, Bavro V, Wilson M, et al. A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans. Metallomics. 2018;10:180-193 pubmed publisher
    ..lividans that serves to preclude deleterious copper levels. This system comprises of several CopZ-like copper chaperones and P1-type ATPases, predominantly under the transcriptional control of a ..
  4. Navarro C, von Bernath D, Martínez Bussenius C, Castillo R, Jerez C. Cytoplasmic CopZ-Like Protein and Periplasmic Rusticyanin and AcoP Proteins as Possible Copper Resistance Determinants in Acidithiobacillus ferrooxidans ATCC 23270. Appl Environ Microbiol. 2016;82:1015-1022 pubmed publisher
    ..Transcriptional expression of A. ferrooxidans genes coding for a cytoplasmic CopZ-like copper-binding chaperone and the periplasmic copper-binding proteins rusticyanin and AcoP, which form part of ..
  5. Garcia S, Du Q, Wu H. Streptococcus mutans copper chaperone, CopZ, is critical for biofilm formation and competitiveness. Mol Oral Microbiol. 2016;31:515-525 pubmed publisher
    ..encodes a negative DNA-binding repressor (CopY), the P1-ATPase copper exporter (CopA), and the copper chaperone (CopZ)...
  6. Lippincott Schwartz J, Liu W. Insights into COPI coat assembly and function in living cells. Trends Cell Biol. 2006;16:e1-4 pubmed
    ..Here, we present images and movies characterizing the dynamics of protein components of the COPI coat in living cells. We discuss the self-assembly of these coat components into a molecular machine for sorting and trafficking membranes. ..
  7. Tamayo A, Bharti A, Trujillo C, Harrison R, Murphy J. COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro. Proc Natl Acad Sci U S A. 2008;105:5254-9 pubmed publisher
    ..This facilitated delivery appears to use a mechanism that is analogous to that of DT entry. ..
  8. Shtutman M, Baig M, Levina E, Hurteau G, Lim C, Broude E, et al. Tumor-specific silencing of COPZ2 gene encoding coatomer protein complex subunit ? 2 renders tumor cells dependent on its paralogous gene COPZ1. Proc Natl Acad Sci U S A. 2011;108:12449-54 pubmed publisher
    ..Function-based genomic screening identified the coatomer protein complex ?1 (COPZ1) gene as essential for different tumor cell types but not for normal cells...
  9. Cukierman E, Huber I, Rotman M, Cassel D. The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science. 1995;270:1999-2002 pubmed
    ..Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism. ..
  10. Kuge O, Hara Kuge S, Orci L, Ravazzola M, Amherdt M, Tanigawa G, et al. zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly. J Cell Biol. 1993;123:1727-34 pubmed
    ..Unlike other coatomer subunits (beta-, beta'-, gamma-, and epsilon-COP), zeta-COP exists in both coatomer bound and free pools. ..
  11. Yu W, Lin J, Jin C, Xia B. Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats. J Mol Biol. 2009;386:903-12 pubmed publisher
    ..These results provide direct evidence supporting the previous proposal that the COP I F-subcomplex and adaptor protein complexes have similar tertiary and quaternary structures. ..
  12. Futatsumori M, Kasai K, Takatsu H, Shin H, Nakayama K. Identification and characterization of novel isoforms of COP I subunits. J Biochem. 2000;128:793-801 pubmed
    ..These results indicate that gamma2-COP and zeta2-COP can form a COP I-like complex in place of gamma1-COP and zeta1-COP, respectively, and suggest that the COP I complex and the COP I-like complex are functionally redundant. ..
  13. Pavel J, Harter C, Wieland F. Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex. Proc Natl Acad Sci U S A. 1998;95:2140-5 pubmed
    ..Herein we describe isolation of a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner. ..
  14. Kotov I, Siebring van Olst E, Knobel P, van der Meulen Muileman I, Felley Bosco E, van Beusechem V, et al. Whole genome RNAi screens reveal a critical role of REV3 in coping with replication stress. Mol Oncol. 2014;8:1747-59 pubmed publisher
    ..Additionally, we found genes related to RS to be significantly enriched among the top hits of the synthetic sickness/lethality (SSL) screen further corroborating the importance of REV3 for DNA replication under conditions of RS. ..
  15. Wegmann D, Hess P, Baier C, Wieland F, Reinhard C. Novel isotypic gamma/zeta subunits reveal three coatomer complexes in mammals. Mol Cell Biol. 2004;24:1070-80 pubmed
    ..This existence of three structurally different forms of coatomer will need to be considered in future models of COPI-mediated transport. ..
  16. Duden R. ER-to-Golgi transport: COP I and COP II function (Review). Mol Membr Biol. 2003;20:197-207 pubmed
    ..Additionally, COP I coat proteins have complex functions in intra-Golgi trafficking and in maintaining the normal structure of the mammalian interphase Golgi complex...
  17. Anania M, Cetti E, Lecis D, Todoerti K, Gulino A, Mauro G, et al. Targeting COPZ1 non-oncogene addiction counteracts the viability of thyroid tumor cells. Cancer Lett. 2017;410:201-211 pubmed publisher
    ..Among those, we found the coatomer protein complex ζ1 (COPZ1) gene, which is involved in intracellular traffic, autophagy and lipid homeostasis...
  18. Faulstich D, Auerbach S, Orci L, Ravazzola M, Wegchingel S, Lottspeich F, et al. Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex. J Cell Biol. 1996;135:53-61 pubmed
    ..We propose that these interactions reflect in vivo associations of those subunits and thus play a functional role in the assembly of coatomer and/or serve to maintain the molecular architecture of the complex. ..
  19. Kay K, Hamilton C, Le Brun N. Mass spectrometry of B. subtilis CopZ: Cu(i)-binding and interactions with bacillithiol. Metallomics. 2016;8:709-19 pubmed publisher
    b>CopZ from Bacillus subtilis is a well-studied member of the highly conserved family of Atx1-like copper chaperones...
  20. Harter C, Wieland F. A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. Proc Natl Acad Sci U S A. 1998;95:11649-54 pubmed
    ..We suggest that, under physiological conditions, interaction of coatomer with both endoplasmic reticulum retrieval motifs and the cytoplasmic domain of p23 is mediated by gamma-COP. ..
  21. Quintana J, Novoa Aponte L, ARGUELLO J. Copper homeostasis networks in the bacterium Pseudomonas aeruginosa. J Biol Chem. 2017;292:15691-15704 pubmed publisher
    ..system) and of a putative Cu+-binding periplasmic chaperone and the unusual presence of two cytoplasmic CopZ proteins. Both CopZ chaperones could bind Cu+ with high affinity...
  22. Li H, Cao L, Yang C, Zhang Z, Zhang B, Deng K. Selective oxidation of benzyl alcohols to benzoic acid catalyzed by eco-friendly cobalt thioporphyrazine catalyst supported on silica-coated magnetic nanospheres. J Environ Sci (China). 2017;60:84-90 pubmed publisher
    A novel magnetically recoverable thioporphyrazine catalyst (CoPz(S-Bu)8/SiO2@Fe3O4) was prepared by immobilization of the cobalt octkis(butylthio) porphyrazine complex (CoPz(S-Bu)8) ..
  23. Moelleken J, Malsam J, Betts M, Movafeghi A, Reckmann I, Meissner I, et al. Differential localization of coatomer complex isoforms within the Golgi apparatus. Proc Natl Acad Sci U S A. 2007;104:4425-30 pubmed
    ..These differences suggest distinct functions for coatomer isoforms in a manner similar to clathrin/adaptor vesicles, where different adaptor proteins serve particular transport routes. ..
  24. Dominguez M, Dejgaard K, Fullekrug J, Dahan S, Fazel A, Paccaud J, et al. gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer. J Cell Biol. 1998;140:751-65 pubmed
    ..Surprisingly, upon expression of mutated members, steady-state distribution of unmutated ones shifted as well, presumably as a consequence of their observed oligomeric properties. ..
  25. Pelham H, Rothman J. The debate about transport in the Golgi--two sides of the same coin?. Cell. 2000;102:713-9 pubmed