- Volume 4 Issue 1
DOI QR Code
A NELL-1 Binding Protein: Vimentin
- Chae, Hwa-Sung (Department of Orthodontics, The Institute of Oral Health Science, Samsung Medical Center, Sung kyunkwan University School of Medicine) ;
- Kim, Young-Ho (Department of Orthodontics, The Institute of Oral Health Science, Samsung Medical Center, Sung kyunkwan University School of Medicine)
- Received : 2011.02.04
- Accepted : 2011.04.20
- Published : 2011.06.30
Purpose: Craniosynostosis (CS), one of the most common congenital craniofacial deformities, is the premature closure of cranial sutures. NELL-1 is a novel molecule overexpressed during premature cranial suture closure in human CS. From a functional perspective, NELL-1 has been reported to accelerate chondrocyte maturation and modulate calvarial osteoblast differentiation and apoptosis pathways. The mechanism through which NELL-1 induces these phenomena, however, remains unclear. The purpose of this study is to identify the NELL-1 binding protein(s) through which the biologic mechanism of NELL-1 can be further investigated. Materials and Methods: Far-Western and Immunoprecipitation (IP) assays were performed, independently and in sequence, followed by mass spectrometry to identify the NELL-1 binding proteins. Reverse IP was used to verify and confirm candidate binding protein. Results: The only confirmative protein from current experimentation was vimentin. Vimentin is the major structural component of the intermediate filaments. Conclusion: The present study identified and confirmed vimentin as a NELL-1 binding protein, which opened up a new window to mechanistically facilitate studies on this CS-associated molecule.
- McGillivray G, Savarirayan R, Cox TC, Stojkoski C, McNeil R, Bankier A, Bateman JF, Roscioli T, Gardner RJ, Lamande SR. Familial scaphocephaly syndrome caused by a novel mutation in the FGFR2 tyrosine kinase domain. J Med Genet. 2005; 142: 656-62.
- Nagase T, Nagase M, Hirose S, Ohmori K. Crouzon synodrome with acanthosis nigricans: a case report and mutational analysis. Cleft Palate Craniofac J. 2000; 137: 78-82.
- Ting K, Vastardis H, Mulliken JB, Soo C, Tieu A, Do H, Kwong E, Bertolami CN, Kawamoto H, Kuroda S, Longaker MT. Human NELL-1 expressed in unilateral coronal synostosis. J Bone Miner Res. 1999; 14: 80-9. https://doi.org/10.1359/jbmr.19184.108.40.206
- Tompkins K, George A, Veis A. Characterization of a mouse amelogenin [A-4]/M59 cell surface receptor. Bone. 2006; 38: 172-80. https://doi.org/10.1016/j.bone.2005.08.013
- Franke WW, Hergt M, Grund C. Rearrangement of the vimentin cytoskeleton during adipose conversion: formation of an intermediate filament cage around lipid globules. Cell. 1987; 49: 131-41. https://doi.org/10.1016/0092-8674(87)90763-X
- Hendrix MJ, Seftor EA, Seftor RE, Trever KT. Experimental coexpression of vimentin and keratin intermediate filaments in human breast cancer cells results in phenotypic interconversion and increased invasive behavior. Am J Pathol. 1997; 150: 483-95.
- Dandachi N, Hauser-Kronberger C, More E, Wiesener B, Hacker GW, Dietze O, Wirl G. Co-expression of tenascin-C and vimentin in human breast cancer cells indicates phenotypic transdifferentiation during tumour progression: correlation with histopathological parameters, hormone receptors, and oncoproteins. J Pathol. 2001; 193: 181-9. https://doi.org/10.1002/1096-9896(2000)9999:9999<::AID-PATH752>3.0.CO;2-V
- Nieminen M, Henttinen T, Merinen M, Marttila-Ichihara F, Eriksson JE, Jalkanen S. Vimentin function in lymphocyte adhesion and transcellular migration. Nat Cell Biol. 2006; 8: 156-62. https://doi.org/10.1038/ncb1355
- Homan SM, Mercurio AM, LaFlamme SE. Endothelial cells assemble two distinct alpha6beta4-containing vimentin-associated structures: roles for ligand binding and the beta4 cytoplasmic tail. J Cell Sci. 1998; 111: 2717-28.
- Gonzales M, Weksler B, Tsuruta D, Goldman RD, Yoon KJ, Hopkinson SB, Flitney FW, Jones JC. Structure and function of a vimentinassociated matrix adhesion in endothelial cells. Mol Biol Cell. 2001; 12: 85-100. https://doi.org/10.1091/mbc.12.1.85
- Tsuruta D, Jones JC. The Vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J Cell Sci. 2003; 116: 4977-84. https://doi.org/10.1242/jcs.00823
- Kreis S, Schönfeld HJ, Melchior C, Steiner B, Kieffer N. The inter-mediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions. Exp Cell Res. 2005; 305: 110-21. https://doi.org/10.1016/j.yexcr.2004.12.023
- Ivaska J, Vuoriluoto K, Huovinen T, Izawa I, Inagaki M, Parker PJ. PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J. 2005; 24: 3834-45. https://doi.org/10.1038/sj.emboj.7600847
- Correia I, Chu D, Chou YH, Goldman RD, Matsudaira P. Integrating the actin and vimentin cytoskeletons:adhesion-dependent formation of fimbrin-vimentin complexes in macrophages. J Cell Biol. 1999; 146: 831-42. https://doi.org/10.1083/jcb.146.4.831
- Sin WC, Chen XQ, Leung T, Lim L. RhoA-binding kinase alpha translocation is facilitated by the collapse of the vimentin intermediate filament network. Mol Cell Biol. 1998; 18: 6325-39. https://doi.org/10.1128/MCB.18.11.6325
- Janosch P, Kieser A, Eulitz M, Lovric J, Sauer G, Reichert M, Gounari F, Büscher D, Baccarini M, Mischak H, Kolch W. The Raf-1 kinase associates with vimentin kinases and regulates the structure of vimentin filaments. FASEB J. 2000; 14: 2008-21. https://doi.org/10.1096/fj.99-0883com
- Perlson E, Hanz S, Ben-Yaakov K, Segal-Ruder Y, Seger R, Fainzilber M. Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron. 2005; 45: 715-26. https://doi.org/10.1016/j.neuron.2005.01.023
- Runembert I, Queffeulou G, Federici P, Vrtovsnik F, Colucci-Guyon E, Babinet C, Briand P, Trugnan G, Friedlander G, Terzi F. Vimentin affects localization and activity of sodium-glucose cotransporter SGLT1 in membrane rafts. J Cell Sci. 2002; 115: 713-24.
- Faigle W, Colucci-Guyon E, Louvard D, Amigorena S, Galli T. Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery. Mol Biol Cell. 2000; 11: 3485-94. https://doi.org/10.1091/mbc.11.10.3485
- Kumar N, Robidoux J, Daniel KW, Guzman G, Floering LM, Collins S. Requirement of vimentin filament assembly for beta3-adrenergic receptor activation of ERK MAP kinase and lipolysis. J Biol Chem. 2007; 282: 9244-50. https://doi.org/10.1074/jbc.M605571200
- Yang X, Wang J, Liu C, Grizzle WE, Yu S, Zhang S, Barnes S, Koopman WJ, Mountz JD, Kimberly RP, Zhang HG. Cleavage of p53-vimentin complex enhances tumor necrosis factor-related apoptosisinducing ligand-mediated apoptosis of rheumatoid arthritis synovial fibroblasts. Am J Pathol. 2005; 167: 705-19. https://doi.org/10.1016/S0002-9440(10)62045-7
- Lopez-Egido J, Cunningham J, Berg M, Oberg K, Bongcam-Rudloff E, Gobl A. Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity. Exp Cell Res. 2002; 278: 175-83. https://doi.org/10.1006/excr.2002.5575
- Schietke R, Bröhl D, Wedig T, Mücke N, Herrmann H, Magin TM. Mutations in vimentin disrupt the cytoskeleton in fibroblasts and delay execution of apoptosis. Eur J Cell Biol. 2006; 85: 1-10.
- Stefanovic S, Windsor M, Nagata KI, Inagaki M, Wileman T. Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. J Virol. 2005; 79: 11766-75. https://doi.org/10.1128/JVI.79.18.11766-11775.2005
- Bhattacharya B, Noad RJ, Roy P. Interaction between Bluetongue virus outer capsid protein VP2 and vimentin is necessary for virus egress. Virol J. 2007; 4: 7-18. https://doi.org/10.1186/1743-422X-4-7
- Ivaska J, Pallari HM, Nevo J, Eriksson JE. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res. 2007; 313: 2050-62. https://doi.org/10.1016/j.yexcr.2007.03.040
- Cowan CM, Cheng S, Ting K, Soo C, Walder B, Wu B, Kuroda S, Zhang X. Nell-1 induced bone formation within the distracted intermaxillary suture. Bone. 2006; 38: 48-58.
- Kuroda S, Tanizawa K. Involvement of epidermal growth factor-like domain of NELL proteins in the novel protein-protein interaction with protein kinase C, Biochem Biophys Res Commun. 1999; 256: 752-7.
- Tolstonog GV, Shoeman RL, Traub U, Traub P. Role of the intermediate filament protein vimentin in delaying senescence and in the spontaneous immortalization of mouse embryo fibroblasts. DNA Cell Biol. 2001; 20: 509-29. https://doi.org/10.1089/104454901317094945
- Andreolas C, Kalogeropoulou M, Voulgari A, Pintzas A. Fra-1 regulates vimentin during Ha-RAS-induced epithelial mesenchymal transition in human colon carcinoma cells. Int J Cancer. 2008; 122: 1745-56.
- Desai J, Hughes L, Millsaps J, Stanford B, Kerley M, Carpenter D, Rinchik E, Culiat C. NELL-1, a gene coding for a novel PKC-binding protein is a candidate for late-gestation recessive lethal mutation at the L7R6 locus. Presented at the 16th international Mouse Genome Conference. 2002; San Antonio (TX).