MEGF9: A novel transmembrane protein with a strong and developmentally regulated expression in the nervous system

Biochemical Journal

Volumn 401, Issue 2, 2007, Pages 447-457

  Brandt Bohne, Ulrike ^a   Keene, Douglas R ^b   White, Fletcher A ^c   Koch, Manuel ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b SHRINERS HOSPITAL FOR CHILDREN   (United States)

^c LOYOLA UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Glial cell; Glycosylation; MEGF9; Nervous system; Skin; Transmembrane protein

Indexed keywords

GLIAL CELLS; GLYCOSYLATION; PERIPHERAL NERVOUS SYSTEM (PNS); TRANSMEMBRANE PROTEINS;

CELLS; MICROSCOPIC EXAMINATION; PROTEINS; REACTION KINETICS; SKIN; TISSUE;

NEUROLOGY;

LAMININ; MEMBRANE PROTEIN; MULTIPLE EPIDERMAL GROWTH FACTOR LIKE DOMAIN 9; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CENTRAL NERVOUS SYSTEM; CONTROLLED STUDY; GASTROINTESTINAL TRACT; GENE EXPRESSION; GLYCOSYLATION; IMMUNOELECTRON MICROSCOPY; IMMUNOHISTOCHEMISTRY; KERATINOCYTE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PERIPHERAL NERVOUS SYSTEM; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; RAT; SKIN EPITHELIUM; TONGUE;

AMINO ACID SEQUENCE; ANIMALS; CENTRAL NERVOUS SYSTEM; EPIDERMAL GROWTH FACTOR; GENE EXPRESSION REGULATION, DEVELOPMENTAL; HUMANS; KERATINOCYTES; MEMBRANE PROTEINS; MICE; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PERIPHERAL NERVOUS SYSTEM; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE ALIGNMENT; SKIN; TONGUE; TUMOR CELLS, CULTURED;

EID: 33846541348     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060691     Document Type: Article

References (31)

1. Campbell, I. D. and Bork, P. (1993) Epidermal growth factor-like modules. Curr. Opin. Struct. Biol. 3, 385-392
2. Engel, J. (1998) EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? FEBS Lett. 231, 1-7
3. Appella, E. W., Weber, I. T. and Blasi, F. (1988) Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett. 231, 1-4
4. Martin, G. R. (1988) Basement membrane proteins: molecular structure and function. Adv. Protein Chem. 39, 1-50
5. Lasky, J. L. and Wu, H. (2005) Notch signaling, brain development, and human disease Pediatr. Res. 57, 104R-109R
6. Fatemi, S. H. (2005) Reelin glycoprotein: structure, biology and roles in health and disease. Mol. Psychiatry 10, 251-257
7. Fan, X., Labrador, J. P., Hing, H. and Bashaw, G. J. (2003) Slit stimulation recruits Dock and Pak to the roundabout receptor and increases Rac activity to regulate axon repulsion at the CNS midline. Neuron 40, 113-127
8. Kusakabe, M., Mangiarini, L., Laywell, E. D., Bates, G. P., Yoshiki, A., Hiraiwa, N., Inoue, J. and Steindler, D. A. (2001) Loss of cortical and thalamic neuronal tenascin-C expression in a transgenic mouse expressing exon 1 of the human Huntington disease gene. J. Comp. Neurol. 430, 485-500
9. Chen, Z. L., Indyk, J. A. and Strickland, S. (2003) The hippocampal laminin matrix is dynamic and critical for neuronal survival. Mol. Biol. Cell 14, 2665-2676
10. de Celis, J. F., Barrio, R., del Arco, A. and Garcia-Bellido, A. (1993) Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 90, 4037-4041
11. Bernardos, R. L., Lentz, S. I., Wolfe, M. S. and Raymond, P. A. (2005) Notch-Delta signaling is required for spatial patterning and Muller glia differentiation in the zebrafish retina. Dev. Biol. 278, 381-395
12. Dowgiert, J., Sosne, G. and Kurpakus-Wheater, M. (2004) Laminin-2 stimulates the proliferation of epithelial cells in a conjunctival epithelial cell line. Cell Prolif. 37, 161-175
13. Haritunians, T., Boulter, J., Hicks, C., Buhrman, J., DiSibio, G., Shawber, C., Weinmaster, G., Nofziger, D. and Schanen, C. (2002) CADASIL Notch3 mutant proteins localize to the cell surface and bind ligand. Circ. Res. 90, 506-508
14. Pilia, G., Uda, M., Macis, D., Frau, F., Crisponi, L., Balli, F., Barbera, C., Colombo, C., Frediani, T., Gatti, R. et al. (1999) Jagged-1 mutation analysis in Italian Alagille syndrome patients. Hum. Mutat. 14, 394-400
15. Webb, J. C., Sun, X. M., McCarthy, S. N., Neuwirth, C., Thompson, G. R., Knight, B. L. and Soutar, A. K. (1996) Characterization of mutations in the low density lipoprotein (LDL)-receptor gene in patients with homozygous familial hypercholesterolemia, and frequency of these mutations in FH patients in the United Kingdom. J. Lipid Res. 37, 368-381
16. Loeys, B., Van Maldergem, L., Mortier, G., Coucke, P., Gerniers, S., Naeyaert, J. M. and De Paepe, A. (2002) Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa. Hum. Mol. Genet. 11, 2113-2118
17. Airenne, T., Haakana, H., Sainio, K., Kallunki, T., Kallunki, P., Sariola, H. and Tryggvason, K. (1996) Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts. Genomics 32, 54-64
18. Koch, M., Murrell, J. R., Hunter, D. D., Olson, P. F., Jin, W., Keene, D. R., Brunken, W. J. and Burgeson, R. E. (2000) A novel member of the netrin family, β-netrin, shares homology with the β-chain of laminin: identification, expression and functional characterization. J. Cell Biol. 151, 221-234
19. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
20. Nakayama, M., Nakajima, D., Nagase, T., Nomura, N., Seki, N. and Ohara, O. (1998) Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening. Genomics 51, 27-34
21. Okazaki, N., Kikuno, R., Ohara, R., Inamoto, S., Koseki, H., Hiraoka, S., Saga, Y., Nagase, T., Ohara, O. and Koga, H. (2003) Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-bomologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries. DNA Res. 10, 167-180
22. Timpl, R. and Brown, J. C. (1994) The laminins. Matrix Biol. 14, 275-81
23. Haltiwanger, R. S. and Lowe, J. B. (2004) Role of glycosylation in development. Annu. Rev. Biochem. 73, 491-537
24. Gendler, S. J. and Spicer, A. R (1995) Epithelial mucin genes. Annu. Rev. Physiol. 57, 607-634
25. Eckhardt, A. E., Timpte, C. S., Abernethy, J. L., Zhao, Y. and Hill, R. L. (1991) Porcine submaxillary mucin contains a cystine-rich, carboxyl-terminal domain in addition to a highly repetitive, glycosylated domain. J. Biol. Chem. 266, 9678-9686
26. Perez-Vilar, J. and Hill, R. L. (1999) The structure and assembly of secreted mucins. J. Biol. Chem. 274, 31751-31754
27. Melnick, M., Chen, H., Zhou, Y. and Jaskoll, T. (2001) An alternatively spliced Muc10 glycoprotein ligand for putative L-selectin binding during mouse embryonic submandibular gland morphogenesis. Arch. Oral Biol. 46, 745-757
28. Michele, D. E. and Campbell, K. P. (2003) Dystropnin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278, 15457-15460
29. Chiu, A. Y., Espinosa de los Monteros, A., Cole, R. A., Loera, S. and de Vellis, J. (1991) Laminin and s-laminin are produced and released by astrocytes, Schwann cells, and schwannomas in culture. Glia 4, 11-24
30. Jessen, K. R. (2004) Glial cells. Int. J. Biochem. Cell Biol. 36, 1861-1867
31. Deiner, M. S. and Sretavan, D. W. (1999) Altered midline axon pathways and ectopic neurons in the developing hypothalamus of netrin-1- and DCC-deficient mice. J. Neurosci. 19, 9900-9912