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Journal articles on the topic 'Cell biology, n.e.c'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Van Langevelde, Arjen, Kees Van Malssen, René Driessen, Kees Goubitz, Frank Hollander, René Peschar, Peter Zwart, and Henk Schenk. "Structure of C n C n+2C n -type (n = even) β′-triacylglycerols." Acta Crystallographica Section B Structural Science 56, no. 6 (December 1, 2000): 1103–11. http://dx.doi.org/10.1107/s0108768100009927.

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The crystal structures of the β′ phase of CLC (1,3-didecanoyl-2-dodecanoylglycerol) and MPM (1,3-ditetradecanoyl-2-hexadecanoylglycerol) have been determined from single-crystal X-ray diffraction and high-resolution X-ray powder diffraction data, respectively. Both these crystals are orthorhombic with space group Iba2 and Z = 8. The unit-cell parameters of β′-CLC are a = 57.368 (6), b = 22.783 (2) and c = 5.6945 (6) Å and the final R value is 0.175. The unit-cell parameters of β′-MPM are a = 76.21 (4), b = 22.63 (1) and c = 5.673 (2) Å and the final Rp value is 0.057. Both the β′-CLC and β′-MPM molecules are crystallized in a chair conformation, having a bend at the glycerol moiety. The zigzag planes of the acyl chains are orthogonally packed, as is typical for a β′ phase. Furthermore, unit-cell parameters of some other members of the C n C n+2C n -type triacylglycerol series have been refined on their high-resolution X-ray powder diffraction pattern. Finally, the crystal structures are compared with the currently known structures and models of triacylglycerols.

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2

Leibovitch, Marie-Pierre, Serge A. Leibovitch, Josette Hillion, Martine Guillier, Annette Schmitz, and Jacques Harel. "Possible role of c-fos, c-N-ras and c-mos proto-oncogenes in muscular development." Experimental Cell Research 170, no. 1 (May 1987): 80–92. http://dx.doi.org/10.1016/0014-4827(87)90118-2.

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3

Miñana, MaDolores, Vicente Felipo, and Santiago Grisolía. "Differential effects of the protein kinase C inhibitors H7 and calphostin C on the cell cycle of neuroblastoma cells." Brain Research 596, no. 1-2 (November 1992): 157–62. http://dx.doi.org/10.1016/0006-8993(92)91543-n.

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4

Yang, Ruojing, and James M. Trevillyan. "c-Jun N-terminal kinase pathways in diabetes." International Journal of Biochemistry & Cell Biology 40, no. 12 (January 2008): 2702–6. http://dx.doi.org/10.1016/j.biocel.2008.06.012.

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5

Krapp, Anne, Vera Saliba-Colombani, and Françoise Daniel-Vedele. "Analysis of C and N metabolisms and of C/N interactions using quantitative genetics." Photosynthesis Research 83, no. 2 (February 2005): 251–63. http://dx.doi.org/10.1007/s11120-004-3196-7.

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6

FORMICKA-KOZLOWSKA, Grazyna, Helga SCHNEIDER-BERNLOHR, Jean-Pierre WARTBURG, and Michael ZEPPEZAUER. "H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase." European Journal of Biochemistry 173, no. 2 (April 1988): 281–85. http://dx.doi.org/10.1111/j.1432-1033.1988.tb13996.x.

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7

GABEN, A., and J. MESTER. "Balb/c 3T3 fibroblasts expressing human estrogen receptor." Cell Biology International Reports 14 (September 1990): 99. http://dx.doi.org/10.1016/0309-1651(90)90498-n.

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8

Sun, Guoming, Shunqian Jin, and R. Baskaran. "MMR/c-Abl-dependent activation of ING2/p73α signaling regulates the cell death response to N-methyl-N′-nitro-N-nitrosoguanidine." Experimental Cell Research 315, no. 18 (November 2009): 3163–75. http://dx.doi.org/10.1016/j.yexcr.2009.09.010.

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9

May, Gerhard H. W., K. Elizabeth Allen, William Clark, Martin Funk, and David A. F. Gillespie. "Analysis of the Interaction between c-Jun and c-Jun N-terminal Kinasein Vivo." Journal of Biological Chemistry 273, no. 50 (December 11, 1998): 33429–35. http://dx.doi.org/10.1074/jbc.273.50.33429.

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10

Wolfman, Janice C., Todd Palmby, Channing J. Der, and Alan Wolfman. "Cellular N-Ras Promotes Cell Survival by Downregulation of Jun N-Terminal Protein Kinase and p38." Molecular and Cellular Biology 22, no. 5 (March 1, 2002): 1589–606. http://dx.doi.org/10.1128/mcb.22.5.1589-1606.2002.

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ABSTRACT Cellular N-Ras provides a steady-state antiapoptotic signal, at least partially through the regulation of phosphorylated Akt and Bad levels. Fibroblasts lacking c-N-Ras expression are highly sensitive to the induction of apoptosis by a variety of agents. Reduction of pBad and pAkt levels using a phosphatidylinositol 3-kinase inhibitor was not sufficient to sensitize the control cell population to the high level of apoptosis observed in the N-Ras knockout cell lines, suggesting that c-N-Ras provides at least one other antiapoptotic signal. Stimulation of the control cells with apoptotic agents results in a transient increase in Jun N-terminal protein kinase (JNK)/p38 activity that decreased to baseline levels during the time course of the experiments. In all cases, however, sustained JNK/p38 activity was observed in cells lacking c-N-Ras expression. This correlated with sustained levels of phosphorylated MKK4 and MKK3/6, upstream activators of JNK and p38, respectively. Mimicking the sustained activation of JNK in the control cells did result in increasing their sensitivity to apoptotic agents, suggesting that prolonged JNK activity is a proapoptotic event. We also examined the potential downstream c-N-Ras targets that might be involved in regulating the duration of the JNK/p38 signal. Only the RalGDS 37G-N-Ras protein protected the N-Ras knockout cells from apoptosis and restored transient rather than sustained JNK activation. These data suggest that cellular N-Ras provides an antiapoptotic signal through at least two distinct mechanisms, one which regulates steady-state pBad and pAkt levels and one which regulates the duration of JNK/p38 activity following an apoptotic challenge.

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11

Al-Hasani, Hadi, Raghu K. Kunamneni, Kevin Dawson, Cynthia S. Hinck, Dirk Müller-Wieland, and Samuel W. Cushman. "Roles of the N- and C-termini of GLUT4 in endocytosis." Journal of Cell Science 115, no. 1 (January 1, 2002): 131–40. http://dx.doi.org/10.1242/jcs.115.1.131.

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In insulin target cells, the predominantly expressed glucose transporter isoform GLUT4 recycles between distinct intracellular compartments and the plasma membrane. To characterize putative targeting signals within GLUT4 in a physiologically relevant cell type, we have analyzed the trafficking of hemagglutinin (HA)-epitope-tagged GLUT4 mutants in transiently transfected primary rat adipose cells. Mutation of the C-terminal dileucine motif (LL489/90) did not affect the cell-surface expression of HA-GLUT4. However, mutation of the N-terminal phenylalanine-based targeting sequence (F5) resulted in substantial increases, whereas deletion of 37 or 28 of the 44 C-terminal residues led to substantial decreases in cell-surface HA-GLUT4 in both the basal and insulin-stimulated states. Studies with wortmannin and coexpression of a dominant-negative dynamin GTPase mutant indicate that these effects appear to be primarily due to decreases and increases, respectively, in the rate of endocytosis. Yeast two-hybrid analyses revealed that the N-terminal phenylalanine-based targeting signal in GLUT4 constitutes a binding site for medium chain adaptins μ1, μ2, and μ3A, implicating a role of this motif in the targeting of GLUT4 to clathrin-coated vesicles.

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12

Yeap, Yvonne Y. C., Ivan H. W. Ng, Bahareh Badrian, Tuong-Vi Nguyen, Yan Y. Yip, Amardeep S. Dhillon, Steven E. Mutsaers, John Silke, Marie A. Bogoyevitch, and Dominic C. H. Ng. "c-Jun N-terminal kinase/c-Jun inhibits fibroblast proliferation by negatively regulating the levels of stathmin/oncoprotein 18." Biochemical Journal 430, no. 2 (August 13, 2010): 345–54. http://dx.doi.org/10.1042/bj20100425.

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The JNKs (c-Jun N-terminal kinases) are stress-activated serine/threonine kinases that can regulate both cell death and cell proliferation. We have developed a cell system to control JNK re-expression at physiological levels in JNK1/2-null MEFs (murine embryonic fibroblasts). JNK re-expression restored basal and stress-activated phosphorylation of the c-Jun transcription factor and attenuated cellular proliferation with increased cells in G1/S-phase of the cell cycle. To explore JNK actions to regulate cell proliferation, we evaluated a role for the cytosolic protein, STMN (stathmin)/Op18 (oncoprotein 18). STMN, up-regulated in a range of cancer types, plays a crucial role in the control of cell division through its regulation of microtubule dynamics of the mitotic spindle. In JNK1/2-null or c-Jun-null MEFs or cells treated with c-Jun siRNA (small interfering RNA), STMN levels were significantly increased. Furthermore, a requirement for JNK/cJun signalling was demonstrated by expression of wild-type c-Jun, but not a phosphorylation-defective c-Jun mutant, being sufficient to down-regulate STMN. Critically, shRNA (small hairpin RNA)-directed STMN down-regulation in JNK1/2-null MEFs attenuated proliferation. Thus JNK/c-Jun regulation of STMN levels provides a novel pathway in regulation of cell proliferation with important implications for understanding the actions of JNK as a physiological regulator of the cell cycle and tumour suppressor protein.

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13

Zumft, W. G. "Cell biology and molecular basis of denitrification." Microbiology and Molecular Biology Reviews 61, no. 4 (December 1997): 533–616. http://dx.doi.org/10.1128/mmbr.61.4.533-616.1997.

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Denitrification is a distinct means of energy conservation, making use of N oxides as terminal electron acceptors for cellular bioenergetics under anaerobic, microaerophilic, and occasionally aerobic conditions. The process is an essential branch of the global N cycle, reversing dinitrogen fixation, and is associated with chemolithotrophic, phototrophic, diazotrophic, or organotrophic metabolism but generally not with obligately anaerobic life. Discovered more than a century ago and believed to be exclusively a bacterial trait, denitrification has now been found in halophilic and hyperthermophilic archaea and in the mitochondria of fungi, raising evolutionarily intriguing vistas. Important advances in the biochemical characterization of denitrification and the underlying genetics have been achieved with Pseudomonas stutzeri, Pseudomonas aeruginosa, Paracoccus denitrificans, Ralstonia eutropha, and Rhodobacter sphaeroides. Pseudomonads represent one of the largest assemblies of the denitrifying bacteria within a single genus, favoring their use as model organisms. Around 50 genes are required within a single bacterium to encode the core structures of the denitrification apparatus. Much of the denitrification process of gram-negative bacteria has been found confined to the periplasm, whereas the topology and enzymology of the gram-positive bacteria are less well established. The activation and enzymatic transformation of N oxides is based on the redox chemistry of Fe, Cu, and Mo. Biochemical breakthroughs have included the X-ray structures of the two types of respiratory nitrite reductases and the isolation of the novel enzymes nitric oxide reductase and nitrous oxide reductase, as well as their structural characterization by indirect spectroscopic means. This revealed unexpected relationships among denitrification enzymes and respiratory oxygen reductases. Denitrification is intimately related to fundamental cellular processes that include primary and secondary transport, protein translocation, cytochrome c biogenesis, anaerobic gene regulation, metalloprotein assembly, and the biosynthesis of the cofactors molybdopterin and heme D1. An important class of regulators for the anaerobic expression of the denitrification apparatus are transcription factors of the greater FNR family. Nitrate and nitric oxide, in addition to being respiratory substrates, have been identified as signaling molecules for the induction of distinct N oxide-metabolizing enzymes.

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14

Dunn, Catherine, Carolyn Wiltshire, Ann MacLaren, and David A. F. Gillespie. "Molecular mechanism and biological functions of c-Jun N-terminal kinase signalling via the c-Jun transcription factor." Cellular Signalling 14, no. 7 (July 2002): 585–93. http://dx.doi.org/10.1016/s0898-6568(01)00275-3.

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15

Aubry, Stéphane, and Jean Charron. "N-Myc Shares Cellular Functions with c-Myc." DNA and Cell Biology 19, no. 6 (June 2000): 353–64. http://dx.doi.org/10.1089/10445490050043326.

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16

See, Raymond H., and Yang Shi. "Adenovirus E1B 19,000-Molecular-Weight Protein Activates c-Jun N-Terminal Kinase and c-Jun-Mediated Transcription." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 4012–22. http://dx.doi.org/10.1128/mcb.18.7.4012.

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ABSTRACT Adenovirus E1B proteins (19,000-molecular-weight [19K] and 55K proteins) inhibit apoptosis and cooperate with adenovirus E1A to induce full oncogenic transformation of primary cells. The E1B 19K protein has previously been shown to be capable of activating transcription; however, the underlying mechanisms are unclear. Here, we show that adenovirus infection activates the c-Jun N-terminal kinase (JNK) and that the E1B gene products are necessary for adenovirus to activate JNK. In transfection assays, we show that the E1B 19K protein is sufficient to activate JNK and can strongly induce c-Jun-dependent transcription. Mapping studies show that the C-terminal portion of E1B 19K is necessary for induction of c-Jun-mediated transcription. Using dominant-negative mutants of several kinases upstream of JNK, we show that MEKK1 and MKK4, but not Ras, are involved in the induction of JNK activity by adenovirus infection. The same dominant-negative kinase mutants also block the ability of E1B 19K to induce c-Jun-mediated transcription. Taken together, these results suggest that E1B 19K may utilize the MEKK1-MKK4-JNK signaling pathway to activate c-Jun-dependent transcription and demonstrate a novel, kinase-activating activity of E1B 19K that may underlie its ability to regulate transcription.

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17

Miyamoto, S., S. Sukumar, R. C. Guzman, R. C. Osborn, and S. Nandi. "Transforming c-Ki-ras mutation is a preneoplastic event in mouse mammary carcinogenesis induced in vitro by N-methyl-N-nitrosourea." Molecular and Cellular Biology 10, no. 4 (April 1990): 1593–99. http://dx.doi.org/10.1128/mcb.10.4.1593-1599.1990.

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Mouse mammary epithelial cells can be transformed in primary cultures to preneoplastic and neoplastic states when treated with N-methyl-N-nitrosourea (MNU). Mammary carcinomas arising from MNU-induced hyperplastic alveolar nodules (a type of mouse mammary preneoplastic lesion) contained transforming c-Ki-ras genes when examined by the NIH 3T3 focus assay. Hybridization of allele-specific oligonucleotides to c-Ki-ras sequences amplified by the polymerase chain reaction demonstrated the presence of a specific G-35----A-35 point mutation in codon 12 in each of the NIH 3T3 foci as well as the mammary carcinomas. This mutation resulted in the substitution of the normal glycine with an aspartic acid. Furthermore, this mutation in the c-Ki-ras proto-oncogenes was also detected in 9 of 10 hyperplastic alveolar nodules. These results demonstrate that the specific c-Ki-ras mutation is a preneoplastic event in MNU-induced mouse mammary carcinogenesis.

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18

Zambetti, Gerard, Anna Ramsey-Ewing, Rita Bortell, Gary Stein, and Janet Stein. "Disruption of the cytoskeleton with cytochalasin D induces c-fos gene expression." Experimental Cell Research 192, no. 1 (January 1991): 93–101. http://dx.doi.org/10.1016/0014-4827(91)90162-n.

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19

Mooney, Lorraine M., and Alan J. Whitmarsh. "Docking Interactions in the c-Jun N-terminal Kinase Pathway." Journal of Biological Chemistry 279, no. 12 (December 29, 2003): 11843–52. http://dx.doi.org/10.1074/jbc.m311841200.

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20

Cain, Stuart A., Andrew K. Baldwin, Yashithra Mahalingam, Bertrand Raynal, Thomas A. Jowitt, C. Adrian Shuttleworth, John R. Couchman, and Cay M. Kielty. "Heparan Sulfate Regulates Fibrillin-1 N- and C-terminal Interactions." Journal of Biological Chemistry 283, no. 40 (July 31, 2008): 27017–27. http://dx.doi.org/10.1074/jbc.m803373200.

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21

Bagowski, Christoph P., Wen Xiong, and James E. Ferrell. "c-Jun N-terminal Kinase Activation inXenopus laevisEggs and Embryos." Journal of Biological Chemistry 276, no. 2 (October 11, 2000): 1459–65. http://dx.doi.org/10.1074/jbc.m008050200.

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22

Miller, Gregory J., Stanley D. Dunn, and Eric H. Ball. "Interaction of the N- and C-terminal Domains of Vinculin." Journal of Biological Chemistry 276, no. 15 (December 21, 2000): 11729–34. http://dx.doi.org/10.1074/jbc.m008646200.

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The vinculin head to tail intramolecular self-association controls its binding sites for other components of focal adhesions. To study this interaction, the head and tail domains were expressed, purified, and assayed for various characteristics of complex formation. Analytical centrifugation demonstrated a strong interaction in solution and formation of a complex more asymmetric than either of the individual domains. A survey of binding conditions using a solid-phase binding assay revealed characteristics of both electrostatic and hydrophobic forces involved in the binding. In addition, circular dichroism of the individual domains and the complex demonstrated that conformational changes likely occur in both domains during association. The interaction sites were more closely mapped on the protein sequence by deletion mutagenesis. Amino acids 181–226, a basic region within the acidic head domain, were identified as a binding site for the vinculin tail, and residues 1009–1066 were identified as sufficient for binding the head. Moreover, mutation of an acidic patch in the tail (residues 1013–1015) almost completely eliminated its ability to interact with the head domain further supporting the significance of ionic interactions in the binding. Our data indicate that the interaction between the head and tail domains of vinculin occurs through oppositely charged contact sites and results in conformational changes in both domains.

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23

Harris, L. L., J. C. Talian, and P. S. Zelenka. "Contrasting patterns of c-myc and N-myc expression in proliferating, quiescent, and differentiating cells of the embryonic chicken lens." Development 115, no. 3 (July 1, 1992): 813–20. http://dx.doi.org/10.1242/dev.115.3.813.

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The present study uses the polymerase chain reaction and in situ hybridization to examine c-myc and N-myc mRNA in the embryonic chicken lens at 6, 10, 14 and 19 days of development and compares the pattern of expression obtained with the developmental pattern of cell proliferation and differentiation. In the central epithelium, c-myc mRNA levels were proportional to the percentage of proliferating cells throughout development. N-myc mRNA expression in this region was relatively low and showed no correlation with cell proliferation. The ratio of N-myc to c-myc mRNA increased markedly with the onset of epithelial cell elongation and terminal fiber cell differentiation, although both c-myc and N-myc mRNAs continued to be expressed in postmitotic, elongating cells of the equatorial epithelium and in terminally differentiating lens fiber cells. Thus, increased expression of N-myc, a gene whose protein product may compete with c-myc protein for dimerization partners, accompanies the dissociation of c-myc expression and cell proliferation during terminal differentiation of lens fiber cells.

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24

Marui, Nobuyuki, Toshiyuki Sakai, Nobuko Hosokawa, Mitsunori Yoshida, Akira Aoike, Keiichi Kawai, Hoyoku Nishino, and Masanori Fukushima. "N-myc suppression and cell cycle arrest at G1 phase by prostaglandins." FEBS Letters 270, no. 1-2 (September 17, 1990): 15–18. http://dx.doi.org/10.1016/0014-5793(90)81224-c.

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25

Small, M. B., N. Hay, M. Schwab, and J. M. Bishop. "Neoplastic transformation by the human gene N-myc." Molecular and Cellular Biology 7, no. 5 (May 1987): 1638–45. http://dx.doi.org/10.1128/mcb.7.5.1638-1645.1987.

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Amplification and abundant expression of a gene known as N-myc are found frequently in advanced stages of human neuroblastoma and may play a role in the genesis of several malignant human tumors. Previous studies have shown that N-myc can cooperate with a mutant allele of the proto-oncogene c-Ha-ras to transform embryonic rat cells in culture. Here we show that N-myc can also act alone to elicit neoplastic growth of an established line of rat fibroblasts (Rat-1). We used recombinant DNA vectors to express either N-myc or its kindred gene c-myc in transfected cells. Both genes caused morphological transformation, anchorage-independent growth, and tumorigenicity. We noticed two variables that appeared to influence the ability to isolate cells transformed by N-myc and c-myc: the abundance in which the genes were expressed and biological selection to eliminate untransformed cells from the cultures. Our findings sustain the belief that N-myc is an authentic proto-oncogene, lend further credibility to the role of N-myc in the genesis of human tumors, and establish a convenient assay that can be used to explore further the properties of both N-myc and c-myc.

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26

Brito, R. M., G. A. Krudy, J. C. Negele, J. A. Putkey, and P. R. Rosevear. "Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C." Journal of Biological Chemistry 268, no. 28 (October 1993): 20966–73. http://dx.doi.org/10.1016/s0021-9258(19)36880-2.

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27

Hardie, Roger C. "Inhibition of phospholipase C activity in Drosophila photoreceptors by 1,2-bis(2-aminophenoxy)ethane N,N,N′,N′-tetraacetic acid (BAPTA) and di-bromo BAPTA." Cell Calcium 38, no. 6 (December 2005): 547–56. http://dx.doi.org/10.1016/j.ceca.2005.07.005.

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28

Laidler, P., and A. Lityńska. "Tumor cell N-glycans in metastasis." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 343–57. http://dx.doi.org/10.18388/abp.1997_4431.

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Metastasis accounts for most of deaths caused by cancer. The increasing body of evidence suggests that changes in N-glycosylation of tumor cell proteins such as increased branching, increased sialylation, polysialylation, decreased fucosylation, enhanced formation of Lewis X and sialyl Lewis X antigens are among important factors determining metastatic potential of tumor cell. Most of the adhesion proteins, e.g., integrins, members of immunoglobulin superfamily, and cadherins are heavily N-glycosylated. The other proteins involved in adhesion, like galectins and type-C selectins, recognize N-glycans as a part of their specific ligands. In this review we focus on recent reports concerning the contribution of N-glycosylation of tumor cell adhesion molecules and some selected membrane proteins in the tumor invasion and metastasis.

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29

Dowd, Marla M., John W. Baynes, and Suzanne R. Thorpe. "Synthesis of N,N-dilactitol ethylenediamine: A versatile spacer for attachment of residualizing labels to protein." Analytical Biochemistry 205, no. 2 (September 1992): 369–71. http://dx.doi.org/10.1016/0003-2697(92)90451-c.

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30

Bull, P., K. L. Morley, M. F. Hoekstra, T. Hunter, and I. M. Verma. "The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain." Molecular and Cellular Biology 10, no. 10 (October 1990): 5473–85. http://dx.doi.org/10.1128/mcb.10.10.5473-5485.1990.

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We have shown that the murine c-rel protein can act as a transcriptional transactivator in both yeast and mammalian cells. Fusion proteins generated by linking rel sequences to the DNA-binding domain of the yeast transcriptional activator GAL4 activate transcription from a reporter gene linked in cis to a GAL4 binding site. The full-length mouse c-rel protein (588 amino acids long) is a poor transactivator; however, the C-terminal portion of the protein between amino acid residues 403 to 568 is a potent transcriptional transactivator. Deletion of the N-terminal half of the c-rel protein augments its transactivation function. We propose that c-rel protein has an N-terminal regulatory domain and a C-terminal transactivation domain which together modulate its function as a transcriptional transactivator.

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31

Nybroe, O., M. Albrechtsen, J. Dahlin, D. Linnemann, J. M. Lyles, C. J. Møller, and E. Bock. "Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C." Journal of Cell Biology 101, no. 6 (December 1, 1985): 2310–15. http://dx.doi.org/10.1083/jcb.101.6.2310.

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The biosynthesis of the neural cell adhesion molecule (N-CAM) was studied in primary cultures of rat cerebral glial cells, cerebellar granule neurons, and skeletal muscle cells. The three cell types produced different N-CAM polypeptide patterns. Glial cells synthesized a 135,000 Mr polypeptide B and a 115,000 Mr polypeptide C, whereas neurons expressed a 200,000 Mr polypeptide A as well as polypeptide B. Skeletal muscle cells produced polypeptide B. The polypeptides synthesized by the three cell types were immunochemically identical. The membrane association of polypeptide C was investigated with methods that distinguish peripheral and integral membrane proteins. Polypeptide C was found to be a peripheral membrane protein, whereas polypeptides A and B were integral membrane proteins with cytoplasmic domains of approximately 50,000 and approximately 25,000 Mr, respectively. The affinity of the membrane binding of polypeptide C increased during postnatal development. The posttranslational modifications of polypeptide C were investigated in glial cell cultures, and it was found to be N-linked glycosylated and sulfated.

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32

van der Hout, Annemarie H., Klaas Kok, Anneke Y. van der Veen, Jan Osinga, Lou F. M. H. de Leij, and Charles H. C. M. Buys. "Localization of amplified c-myc and n-myc in small cell lung cancer cell lines." Cancer Genetics and Cytogenetics 38, no. 1 (March 1989): 1–8. http://dx.doi.org/10.1016/0165-4608(89)90158-1.

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33

Rzeczkowski, Katharina, Knut Beuerlein, Helmut Müller, Oliver Dittrich-Breiholz, Heike Schneider, Daniela Kettner-Buhrow, Helmut Holtmann, and Michael Kracht. "c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies." Journal of Cell Biology 194, no. 4 (August 22, 2011): 581–96. http://dx.doi.org/10.1083/jcb.201006089.

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Cytokines and stress-inducing stimuli signal through c-Jun N-terminal kinase (JNK) using a diverse and only partially defined set of downstream effectors. In this paper, the decapping complex subunit DCP1a was identified as a novel JNK target. JNK phosphorylated DCP1a at residue S315 in vivo and in vitro and coimmunoprecipitated and colocalized with DCP1a in processing bodies (P bodies). Sustained JNK activation by several different inducers led to DCP1a dispersion from P bodies, whereas IL-1 treatment transiently increased P body number. Inhibition of TAK1–JNK signaling also affected the number and size of P bodies and the localization of DCP1a, Xrn1, and Edc4. Transcriptome analysis further identified a central role for DCP1a in IL-1–induced messenger ribonucleic acid (mRNA) expression. Phosphomimetic mutation of S315 stabilized IL-8 but not IκBα mRNA, whereas overexpressed DCP1a blocked IL-8 transcription and suppressed p65 NF-κB nuclear activity. Collectively, these data reveal DCP1a as a multifunctional regulator of mRNA expression and suggest a novel mechanism controlling the subcellular localization of DCP1a in response to stress or inflammatory stimuli.

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34

Papadimitriou, E., M. Heroult, J. Courty, A. Polykratis, C. Stergiou, and P. Katsoris. "Endothelial Cell Proliferation Induced by HARP: Implication of N or C Terminal Peptides." Biochemical and Biophysical Research Communications 274, no. 1 (July 2000): 242–48. http://dx.doi.org/10.1006/bbrc.2000.3126.

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35

MacCorkle-Chosnek, Rebecca A., Aaron VanHooser, David W. Goodrich, B. R. Brinkley, and Tse-Hua Tan. "Cell Cycle Regulation of c-Jun N-Terminal Kinase Activity at the Centrosomes." Biochemical and Biophysical Research Communications 289, no. 1 (November 2001): 173–80. http://dx.doi.org/10.1006/bbrc.2001.5948.

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36

Piotrowski, Markus, Tim Janowitz, and Helmut Kneifel. "Plant C-N Hydrolases and the Identification of a Plant N-Carbamoylputrescine Amidohydrolase Involved in Polyamine Biosynthesis." Journal of Biological Chemistry 278, no. 3 (November 14, 2002): 1708–12. http://dx.doi.org/10.1074/jbc.m205699200.

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37

Takatsu, Yoshihiro, Makoto Nakamura, Mark Stapleton, Maria C. Danos, Kunihiro Matsumoto, Michael B. O'Connor, Hiroshi Shibuya, and Naoto Ueno. "TAK1 Participates in c-Jun N-Terminal Kinase Signaling during Drosophila Development." Molecular and Cellular Biology 20, no. 9 (May 1, 2000): 3015–26. http://dx.doi.org/10.1128/mcb.20.9.3015-3026.2000.

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ABSTRACT Transforming growth factor β (TGF-β)-activated kinase 1 (TAK1) is a member of the MAPKKK superfamily and has been characterized as a component of the TGF-β/bone morphogenetic protein signaling pathway. TAK1 function has been extensively studied in cultured cells, but its in vivo function is not fully understood. In this study, we isolated aDrosophila homolog of TAK1 (dTAK1) which contains an extensively conserved NH2-terminal kinase domain and a partially conserved COOH-terminal domain. To learn about possible endogenous roles of TAK1 during animal development, we generated transgenic flies which express dTAK1 or the mouseTAK1 (mTAK1) gene in the fly visual system. Ectopic activation of TAK1 signaling leads to a small eye phenotype, and genetic analysis reveals that this phenotype is a result of ectopically induced apoptosis. Genetic and biochemical analyses also indicate that the c-Jun amino-terminal kinase (JNK) signaling pathway is specifically activated by TAK1 signaling. Expression of a dominant negative form of dTAK during embryonic development resulted in various embryonic cuticle defects including dorsal open phenotypes. Our results strongly suggest that in Drosophila melanogaster, TAK1 functions as a MAPKKK in the JNK signaling pathway and participates in such diverse roles as control of cell shape and regulation of apoptosis.

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38

Zhou, Mo, Heidi Wiener, Wenjuan Su, Yong Zhou, Caroline Liot, Ian Ahearn, John F. Hancock, and Mark R. Philips. "VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking." Journal of Cell Biology 214, no. 4 (August 8, 2016): 445–58. http://dx.doi.org/10.1083/jcb.201604061.

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Ras guanosine triphosphatases (GTPases) regulate signaling pathways only when associated with cellular membranes through their C-terminal prenylated regions. Ras proteins move between membrane compartments in part via diffusion-limited, fluid phase transfer through the cytosol, suggesting that chaperones sequester the polyisoprene lipid from the aqueous environment. In this study, we analyze the nature of the pool of endogenous Ras proteins found in the cytosol. The majority of the pool consists of farnesylated, but not palmitoylated, N-Ras that is associated with a high molecular weight (HMW) complex. Affinity purification and mass spectrographic identification revealed that among the proteins found in the HMW fraction is VPS35, a latent cytosolic component of the retromer coat. VPS35 bound to N-Ras in a farnesyl-dependent, but neither palmitoyl- nor guanosine triphosphate (GTP)–dependent, fashion. Silencing VPS35 increased N-Ras’s association with cytoplasmic vesicles, diminished GTP loading of Ras, and inhibited mitogen-activated protein kinase signaling and growth of N-Ras–dependent melanoma cells.

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39

Dobrzanski, P., R. P. Ryseck, and R. Bravo. "Both N- and C-terminal domains of RelB are required for full transactivation: role of the N-terminal leucine zipper-like motif." Molecular and Cellular Biology 13, no. 3 (March 1993): 1572–82. http://dx.doi.org/10.1128/mcb.13.3.1572-1582.1993.

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RelB, a member of the Rel family of transcription factors, can stimulate promoter activity in the presence of p50-NF-kappa B or p50B/p49-NF-kappa B in mammalian cells. Transcriptional activation analysis reveals that the N and C termini of RelB are required for full transactivation in the presence of p50-NF-kappa B. RelB/p50-NF-kappa B hybrid molecules containing the Rel homology domain of p50-NF-kappa B and the N and C termini of RelB have high transcriptional activity compared with wild-type p50-NF-kappa B. The N and C termini of RelB cooperate in transactivation in cis or trans configuration. Alterations in the structure of the leucine zipper-like motif present in the N terminus of RelB significantly decrease the transcriptional capacity of RelB and of different RelB/p50-NF-kappa B hybrid molecules.

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40

BLUME, Astrid, Wenke WEIDEMANN, Ulrich STELZL, Erich E. WANKER, Lothar LUCKA, Peter DONNER, Werner REUTTER, Rüdiger HORSTKORTE, and Stephan HINDERLICH. "Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase." Biochemical Journal 384, no. 3 (December 7, 2004): 599–607. http://dx.doi.org/10.1042/bj20040917.

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UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a bifunctional enzyme, which initiates and regulates sialic acid biosynthesis. Sialic acids are important compounds of mammalian glycoconjugates, mediating several biological processes, such as cell–cell or cell–matrix interactions. In order to characterize the function of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, a number of deletion mutants were generated, lacking either parts of the N-terminal epimerase or the C-terminal kinase domain. N-terminal deletion of only 39 amino acids results in a complete loss of epimerase activity. Deletions in the C-terminal part result in a reduction or complete loss of kinase activity, depending on the size of the deletion. Deletions at either the N- or the C-terminus also result in a reduction of the other enzyme activity. These results indicate that a separate expression of both domains is possible, but that a strong intramolecular dependency of the two domains has arisen during evolution of the enzyme. N-terminal, as well as C-terminal, mutants tend to form trimers, in addition to the hexameric structure of the native enzyme. These results and yeast two-hybrid experiments show that structures required for dimerization are localized within the kinase domain, and a potential trimerization site is possibly located in a region between the two domains. In conclusion, our results reveal that the activities, as well as the oligomeric structure, of this bifunctional enzyme seem to be organized and regulated in a complex manner.

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Kubota, Yoshihisa, Sun Hee Kim, Sanae M. M. Iguchi-Ariga, and Hiroyoshi Ariga. "Transrepression of the N-myc expression by c-myc protein." Biochemical and Biophysical Research Communications 162, no. 3 (August 1989): 991–97. http://dx.doi.org/10.1016/0006-291x(89)90771-7.

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42

Wong, Kenneth, Xue-Bin Li, and Nicole Hunchuk. "N-Acetylsphingosine (C-ceramide) Inhibited Neutrophil Superoxide Formation and Calcium Influx." Journal of Biological Chemistry 270, no. 7 (February 17, 1995): 3056–62. http://dx.doi.org/10.1074/jbc.270.7.3056.

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Fujita, Yasuyuki, Takuya Sasaki, Koji Fukui, Hirokazu Kotani, Toshihiro Kimura, Yutaka Hata, Thomas C. Südhof, Richard H. Scheller, and Yoshimi Takai. "Phosphorylation of Munc-18/n-Sec1/rbSec1 by Protein Kinase C." Journal of Biological Chemistry 271, no. 13 (March 29, 1996): 7265–68. http://dx.doi.org/10.1074/jbc.271.13.7265.

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44

Wolfman, Janice C., and Alan Wolfman. "Endogenous c-N-Ras Provides a Steady-state Anti-apoptotic Signal." Journal of Biological Chemistry 275, no. 25 (April 20, 2000): 19315–23. http://dx.doi.org/10.1074/jbc.m000250200.

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45

Chong, Huira, and Kun-Liang Guan. "Regulation of Raf through Phosphorylation and N Terminus-C Terminus Interaction." Journal of Biological Chemistry 278, no. 38 (July 14, 2003): 36269–76. http://dx.doi.org/10.1074/jbc.m212803200.

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46

Solanas, Guiomar, Susana Miravet, David Casagolda, Julio Castaño, Imma Raurell, Ana Corrionero, Antonio García de Herreros, and Mireia Duñach. "β-Catenin and Plakoglobin N- and C-tails Determine Ligand Specificity." Journal of Biological Chemistry 279, no. 48 (September 20, 2004): 49849–56. http://dx.doi.org/10.1074/jbc.m408685200.

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47

Tao, Nengbing, Steven J. Wagner, and Douglas M. Lublin. "CD36 Is Palmitoylated on Both N- and C-terminal Cytoplasmic Tails." Journal of Biological Chemistry 271, no. 37 (September 13, 1996): 22315–20. http://dx.doi.org/10.1074/jbc.271.37.22315.

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48

Jones, Emma V., Mark J. Dickman, and Alan J. Whitmarsh. "Regulation of p73-mediated apoptosis by c-Jun N-terminal kinase." Biochemical Journal 405, no. 3 (July 13, 2007): 617–23. http://dx.doi.org/10.1042/bj20061778.

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The JNK (c-Jun N-terminal kinase)/mitogen-activated protein kinase signalling pathway is a major mediator of stress responses in cells, including the response to DNA damage. DNA damage also causes the stabilization and activation of p73, a member of the p53 family of transcription factors. p73, like p53, can mediate apoptosis by up-regulating the expression of pro-apoptotic genes, including Bax (Bcl2-associated X protein) and PUMA (p53 up-regulated modulator of apoptosis). Changes in p73 expression have been linked to tumour progression, particularly in neuroblastomas, whereas in tumours that feature inactivated p53 there is evidence that p73 may mediate the apoptotic response to chemotherapeutic agents. In the present study, we demonstrate a novel link between the JNK signalling pathway and p73. We use pharmacological and genetic approaches to show that JNK is required for p73-mediated apoptosis induced by the DNA damaging agent cisplatin. JNK forms a complex with p73 and phosphorylates it at several serine and threonine residues. The mutation of JNK phosphorylation sites in p73 abrogates cisplatin-induced stabilization of p73 protein, leading to a reduction in p73 transcriptional activity and reduced p73-mediated apoptosis. Our results demonstrate that the JNK pathway is an important regulator of DNA damage-induced apoptosis mediated by p73.

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Solanas, Guiomar, Susana Miravet, David Casagolda, Julio Castaño, Imma Raurell, Ana Corrionero, Antonio García de Herreros, and Mireia Duñach. "β-Catenin and plakoglobin N- and C-tails determine ligand specificity." Journal of Biological Chemistry 291, no. 46 (November 11, 2016): 23925–27. http://dx.doi.org/10.1074/jbc.a116.408685.

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50

Campeau, Eric, and Roy A. Gravel. "Expression inEscherichia coliof N- and C-terminally Deleted Human Holocarboxylase Synthetase." Journal of Biological Chemistry 276, no. 15 (December 21, 2000): 12310–16. http://dx.doi.org/10.1074/jbc.m009717200.

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Biotin functions as a covalently bound cofactor of biotindependent carboxylases. Biotin attachment is catalyzed by biotin protein ligases, called holocarboxylase synthetase in mammals and BirA in prokaryotes. These enzymes show a high degree of sequence similarity in their biotinylation domains but differ markedly in the length and sequence of their N terminus. BirA is also the repressor of the biotin operon, and its DNA attachment site is located in its N terminus. The function of the eukaryotic N terminus is unknown. Holocarboxylase synthetase with N- and C-terminal deletions were evaluated for the ability to catalyze biotinylation after expression inEscherichia coliusing bacterial and human acceptor substrates. We showed that the minimum functional protein is comprised of the last 349 of the 726-residue protein, which includes the biotinylation domain. Significantly, enzyme containing intermediate length, N-terminal deletions interfered with biotin transfer and interaction with different peptide acceptor substrates. We propose that the N terminus of holocarboxylase synthetase contributes to biotinylation through N- and C-terminal interactions and may affect acceptor substrate recognition. Our findings provide a rationale for the biotin responsiveness of patients with point mutations in the N-terminal sequence of holocarboxylase synthetase. Such mutant enzyme may respond to biotin-mediated stabilization of the substrate-bound complex.

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