Disease relevance of CEP110

• NIN, a gene encoding a CEP110-like centrosomal protein, is fused to PDGFRB in a patient with a t(5;14)(q33;q24) and an imatinib-responsive myeloproliferative disorder [1].
• Ninety-one percent of NCCTG gliomas with 1p/19q deletion and 12% without 1p/19q deletion had CEP1/19p12 fusion (P < 0.001, chi(2) test) [2].
• Among NCCTG patients, CEP1/19p12 fusion prevalence was 55%, 47%, and 0% among the oligodendrogliomas, mixed oligoastrocytomas, and astrocytomas, respectively [2].
• Between January 1985 and May 1988, 87 patients with stage III-IV ovarian carcinoma were entered in a study assessing chemotherapy consisting of cyclophosphamide, 500 mg/m2, epirubicin, 75 mg/m2, and cisplatin, 50 mg/m2, intravenously (IV) on day 1, every 4 weeks (CEP-1) [3].
• We studied the interaction of RU 51746-2 with CEP-1 in an E. coli C600 derivative containing pNU104, a multicopy plasmid in which an up-promoter mutation has increased the level of beta-lactamase expression [4].

High impact information on CEP110

• We report here the cloning of the t(8;9)(p12;q33) and the detection of a novel fusion betweenFGFR1 and the CEP110 gene, which codes for a novel centrosome-associated protein with a unique cell-cycle distribution [5].
• CEP110 is widely expressed at various levels in different tissues and is predicted to encode a 994-amino acid coiled-coil protein with 4 consensus leucine zippers [L-X(6)-L-X(6)-L-X(6)-L] [5].
• CEP1/19p12 fusion was observed in all metaphases and 74% of interphase nuclei [2].
• Interphase fusion of CEP1 and 19p12 probes detected the t(1;19) [2].
• In this study, the centrosomal proteins CEP110 and ninein were mapped in relationship to the tubular configuration [6].

Biological context of CEP110

• Further, microinjection of antibodies to either CEP110 or ninein into metaphase PtK2 cells not only disrupted the tubular configuration within the centrosome but also affected the centrosome's ability to function as a microtubule organizing center (MTOC) [6].
• A biphenotypic transformation of 8p11 myeloproliferative syndrome with CEP1/FGFR1 fusion gene [7].
• Of relevant importance is that fasn-1 is the first CEP-1 direct target gene identified so far in C. elegans and our results suggest a new CEP-1 role in cellular proliferation and development, besides the one already described in apoptosis of germ cells [8].

Anatomical context of CEP110

• Importantly, the appearance of CEP110 and ninein at the open end of the daughter centrosome occurred during the telophase-G1 transition of the next cell cycle, concomitant with the maturation of the daughter centrosome into a mother centrosome [6].
• Microinjection of antibodies against either CEP110 or ninein into metaphase HeLa cells disrupted the reformation of the tubular conformation of proteins within the centrosome following cell division and consequently led to dispersal of centrosomal material throughout the cytosol [6].

Associations of CEP110 with chemical compounds

• Strains producing TEM-2 and CEP-1 were resistant to LY163892, cefaclor and cephalexin [9].
• Organisms producing these beta-lactamases, but not TEM-2 and CEP-1, appeared to be more susceptible to LY163892 than cephalexin, although cephalexin proved to be more resistant to beta-lactamase activity [9].
• Interaction with CEP-1 beta-lactamase of RU 51746-2, the active form of the new oral cephalosporin RU 51807 [4].

Other interactions of CEP110

• For two patients with a t(8;9), we found that CEP110 exon 15 was fused to FGFR1 exon 9 [10].
• We show that CEP-1, the C. elegans p53 homolog, is able to bind the two p53 family responsive elements (REs) identified in the worm fasn-1 gene [8].

References