|
1. Akashi, K., Traver, D., Miyamoto, T. and Weissman, I.L. A clonogenic common myeloid progenitor that gives rise to all myeloid lineages. Nature 404, 193-197 (2000).
2. Debili, N., Coulombel, L., Croisille, L., Katz, A., Guichard, J., Breton-Gorius, J., et al. Characterization of a bipotent erythro-megakaryocytic progenitor in human bone marrow. Blood 88, 1284-1296 (1996).
3. Ravid, K., Lu, J., Zimmet, J.M. and Jones, M.R. Roads to polyploidy: the megakaryocyte example. J Cell Physiol 190, 7-20 (2002).
4. Raslova, H. Megakaryocyte polyploidization is associated with a functional gene amplification. Blood 101, 541-544 (2002).
5. Schulze, H. and Shivdasani, R.A. Molecular mechanisms of megakaryocyte differentiation. Semin Thromb Hemost 30, 389-398 (2004).
6. Kaushansky, K. Historical review: megakaryopoiesis and thrombopoiesis. Blood 111, 981-986 (2007).
7. Avecilla, S.T., Hattori, K., Heissig, B., Tejada, R., Liao, F., Shido, K., et al. Chemokine-mediated interaction of hematopoietic progenitors with the bone marrow vascular niche is required for thrombopoiesis. Nat Med 10, 64-71 (2003).
8. Kirito, K. and Kaushansky, K. Transcriptional regulation of megakaryopoiesis: thrombopoietin signaling and nuclear factors. Curr Opin Hematol 13, 151-156 (2006).
9. Kaushansky, K. Thrombopoietin and the Hematopoietic Stem Cell. Ann N Y Acad Sci 1044, 139-141 (2005).
10. Kaushansky, K. Lineage-specific hematopoietic growth factors. N Engl J Med 354, 2034-2045 (2006).
11. Kaushansky, K. The molecular mechanisms that control thrombopoiesis. Journal of Clinical Investigation 115, 3339-3347 (2005).
12. Kaushansky, K., Lok, S., Holly, R.D., Broudy, V.C., Lin, N., Bailey, M.C., et al. Promotion of megakaryocyte progenitor expansion and differentiation by the c-Mpl ligand thrombopoietin. Nature 369, 568-571 (1994).
13. Szalai, G., LaRue, A.C. and Watson, D.K. Molecular mechanisms of megakaryopoiesis. Cellular and Molecular Life Sciences 63, 2460-2476 (2006).
14. Shivdasani, R.A., Fujiwara, Y., McDevitt, M.A. and Orkin, S.H. A lineage-selective knockout establishes the critical role of transcription factor GATA-1 in megakaryocyte growth and platelet development. EMBO J 16, 3965-3973 (1997).
15. Fujiwara, Y., Browne, C.P., Cunniff, K., Goff, S.C. and Orkin, S.H. Arrested development of embryonic red cell precursors in mouse embryos lacking transcription factor GATA-1. Proc Natl Acad Sci U S A 93, 12355-12358 (1996).
16. Lemarchandel, V., Ghysdael, J., Mignotte, V., Rahuel, C. and Romeo, P.H. GATA and Ets cis-acting sequences mediate megakaryocyte-specific expression. Mol Cell Biol 13, 668-676 (1993).
17. Deveaux, S., Filipe, A., Lemarchandel, V., Ghysdael, J., Romeo, P.H. and Mignotte, V. Analysis of the thrombopoietin receptor (MPL) promoter implicates GATA and Ets proteins in the coregulation of megakaryocyte-specific genes. Blood 87, 4678-4685 (1996).
18. Eisbacher, M., Holmes, M.L., Newton, A., Hogg, P.J., Khachigian, L.M., Crossley, M., et al. Protein-Protein Interaction between Fli-1 and GATA-1 Mediates Synergistic Expression of Megakaryocyte-Specific Genes through Cooperative DNA Binding. Molecular and Cellular Biology 23, 3427-3441 (2003).
19. Wang, X., Crispino, J.D., Letting, D.L., Nakazawa, M., Poncz, M. and Blobel, G.A. Control of megakaryocyte-specific gene expression by GATA-1 and FOG-1: role of Ets transcription factors. EMBO J 21, 5225-5234 (2002).
20. Lozzio, C.B. and Lozzio, B.B. Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome. Blood 45, 321-334 (1975).
21. Lozzio, B.B., Lozzio, C.B., Bamberger, E.G. and Feliu, A.S. A multipotential leukemia cell line (K-562) of human origin. Proc Soc Exp Biol Med 166, 546-550 (1981).
22. Tsiftsoglou, A.S., Pappas, I.S. and Vizirianakis, I.S. Mechanisms involved in the induced differentiation of leukemia cells. Pharmacology &; Therapeutics 100, 257-290 (2003).
23. Racke, F.K., Lewandowska, K., Goueli, S. and Goldfarb, A.N. Sustained activation of the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway is required for megakaryocytic differentiation of K562 cells. J Biol Chem 272, 23366-23370 (1997).
24. Whalen, A.M., Galasinski, S.C., Shapiro, P.S., Nahreini, T.S. and Ahn, N.G. Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase. Mol Cell Biol 17, 1947-1958 (1997).
25. Herrera, R., Hubbell, S., Decker, S. and Petruzzelli, L. A role for the MEK/MAPK pathway in PMA-induced cell cycle arrest: modulation of megakaryocytic differentiation of K562 cells. Exp Cell Res 238, 407-414 (1998).
26. Goldfarb, A.N. Stromal Inhibition of Megakaryocytic Differentiation Correlates with Blockade of Signaling by Protein Kinase C-epsilon and ERK/MAPK. Journal of Biological Chemistry 276, 29526-29530 (2001).
27. Sakurai, T., Yamada, T., Kihara-Negishi, F., Teramoto, S., Sato, Y., Izawa, T., et al. Effects of overexpression of the Ets family transcription factor TEL on cell growth and differentiation of K562 cells. Int J Oncol 22, 1327-1333 (2003).
28. Holmes, M.L. Cloning and Analysis of the Thrombopoietin-induced Megakaryocyte-specific Glycoprotein VI Promoter and Its Regulation by GATA-1, Fli-1, and Sp1. Journal of Biological Chemistry 277, 48333-48341 (2002).
29. Athanasiou, M., Clausen, P.A., Mavrothalassitis, G.J., Zhang, X.K., Watson, D.K. and Blair, D.G. Increased expression of the ETS-related transcription factor FLI-1/ERGB correlates with and can induce the megakaryocytic phenotype. Cell Growth Differ 7, 1525-1534 (1996).
30. Alitalo, R. Induced differentiation of K562 leukemia cells: a model for studies of gene expression in early megakaryoblasts. Leuk Res 14, 501-514 (1990).
31. Raman, M., Chen, W. and Cobb, M.H. Differential regulation and properties of MAPKs. Oncogene 26, 3100-3112 (2007).
32. Krishna, M. and Narang, H. The complexity of mitogen-activated protein kinases (MAPKs) made simple. Cell Mol Life Sci 65, 3525-3544 (2008).
33. Shelly, C., Petruzzelli, L. and Herrera, R. PMA-induced phenotypic changes in K562 cells: MAPK-dependent and -independent events. Leukemia 12, 1951-1961 (1998).
34. Jiang, F., Jia, Y. and Cohen, I. Fibronectin- and protein kinase C-mediated activation of ERK/MAPK are essential for proplateletlike formation. Blood 99, 3579-3584 (2002).
35. Jacquel, A., Herrant, M., Defamie, V., Belhacene, N., Colosetti, P., Marchetti, S., et al. A survey of the signaling pathways involved in megakaryocytic differentiation of the human K562 leukemia cell line by molecular and c-DNA array analysis. Oncogene 25, 781-794 (2005).
36. Evans, R.M. Vimentin: the conundrum of the intermediate filament gene family. Bioessays 20, 79-86 (1998).
37. Fuchs, E. and Weber, K. Intermediate filaments: structure, dynamics, function, and disease. Annu Rev Biochem 63, 345-382 (1994).
38. Chang, L. and Goldman, R.D. Intermediate filaments mediate cytoskeletal crosstalk. Nat Rev Mol Cell Biol 5, 601-613 (2004).
39. Ivaska, J., Pallari, H.-M., Nevo, J. and Eriksson, J.E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res 313, 2050-2062 (2007).
40. Colucci-Guyon, E., Portier, M.M., Dunia, I., Paulin, D., Pournin, S. and Babinet, C. Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79, 679-694 (1994).
41. Colucci-Guyon, E., Gimenez, Y.R.M., Maurice, T., Babinet, C. and Privat, A. Cerebellar defect and impaired motor coordination in mice lacking vimentin. Glia 25, 33-43 (1999).
42. Eckes, B., Colucci-Guyon, E., Smola, H., Nodder, S., Babinet, C., Krieg, T., et al. Impaired wound healing in embryonic and adult mice lacking vimentin. J Cell Sci 113 ( Pt 13), 2455-2462 (2000).
43. Eckes, B., Dogic, D., Colucci-Guyon, E., Wang, N., Maniotis, A., Ingber, D., et al. Impaired mechanical stability, migration and contractile capacity in vimentin-deficient fibroblasts. J Cell Sci 111 ( Pt 13), 1897-1907 (1998).
44. Nieminen, M., Henttinen, T., Merinen, M., Marttila–Ichihara, F., Eriksson, J.E. and Jalkanen, S. Vimentin function in lymphocyte adhesion and transcellular migration. Nat Cell Biol 8, 156-162 (2006).
45. Maemura, M., Akiyama, S.K., Woods, V.L., Jr. and Dickson, R.B. Expression and ligand binding of alpha 2 beta 1 integrin on breast carcinoma cells. Clin Exp Metastasis 13, 223-235 (1995).
46. Vincent, P.A., Xiao, K., Buckley, K.M. and Kowalczyk, A.P. VE-cadherin: adhesion at arm's length. Am J Physiol Cell Physiol 286, C987-997 (2004).
47. Green, K.J., Bohringer, M., Gocken, T. and Jones, J.C. Intermediate filament associated proteins. Adv Protein Chem 70, 143-202 (2005).
48. Homan, S.M., Mercurio, A.M. and LaFlamme, S.E. Endothelial cells assemble two distinct alpha6beta4-containing vimentin-associated structures: roles for ligand binding and the beta4 cytoplasmic tail. J Cell Sci 111 ( Pt 18), 2717-2728 (1998).
49. Ivaska, J., Vuoriluoto, K., Huovinen, T., Izawa, I., Inagaki, M. and Parker, P.J. PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J 24, 3834-3845 (2005).
50. Perlson, E., Michaelevski, I., Kowalsman, N., Ben-Yaakov, K., Shaked, M., Seger, R., et al. Vimentin Binding to Phosphorylated Erk Sterically Hinders Enzymatic Dephosphorylation of the Kinase. J Mol Biol 364, 938-944 (2006).
51. Perlson, E., Hanz, S., Ben-Yaakov, K., Segal-Ruder, Y., Seger, R. and Fainzilber, M. Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron 45, 715-726 (2005).
52. Tzivion, G. Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo. Journal of Biological Chemistry 275, 29772-29778 (2000).
53. Tang, D.D. Intermediate filaments in smooth muscle. Am J Physiol Cell Physiol 294, C869-878 (2008).
54. Minin, A.A. and Moldaver, M.V. Intermediate vimentin filaments and their role in intracellular organelle distribution. Biochemistry (Mosc) 73, 1453-1466 (2008).
55. Ralton, J.E., Lu, X., Hutcheson, A.M. and Quinlan, R.A. Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein. J Cell Sci 107 ( Pt 7), 1935-1948 (1994).
56. Herrmann, H., Bar, H., Kreplak, L., Strelkov, S.V. and Aebi, U. Intermediate filaments: from cell architecture to nanomechanics. Nat Rev Mol Cell Biol 8, 562-573 (2007).
57. Steinert, P.M., Marekov, L.N. and Parry, D.A. Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J Biol Chem 268, 24916-24925 (1993).
58. Herrmann, H. and Aebi, U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu Rev Biochem 73, 749-789 (2004).
59. Herrmann, H. and Aebi, U. Intermediate filaments and their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr Opin Cell Biol 12, 79-90 (2000).
60. Styers, M.L., Kowalczyk, A.P. and Faundez, V. Intermediate filaments and vesicular membrane traffic: the odd couple's first dance? Traffic 6, 359-365 (2005).
61. Parry, D.A., Crewther, W.G., Fraser, R.D. and MacRae, T.P. Structure of alpha-keratin: structural implication of the amino acid sequences of the type I and type II chain segments. J Mol Biol 113, 449-454 (1977).
62. McLachlan, A.D. and Stewart, M. Periodic charge distribution in the intermediate filament proteins desmin and vimentin. J Mol Biol 162, 693-698 (1982).
63. Meng, J.J., Khan, S. and Ip, W. Charge interactions in the rod domain drive formation of tetramers during intermediate filament assembly. J Biol Chem 269, 18679-18685 (1994).
64. Shoeman, R.L., Hartig, R., Berthel, M. and Traub, P. Deletion mutagenesis of the amino-terminal head domain of vimentin reveals dispensability of large internal regions for intermediate filament assembly and stability. Exp Cell Res 279, 344-353 (2002).
65. Steinert, P.M., Idler, W.W., Cabral, F., Gottesman, M.M. and Goldman, R.D. In vitro assembly of homopolymer and copolymer filaments from intermediate filament subunits of muscle and fibroblastic cells. Proc Natl Acad Sci U S A 78, 3692-3696 (1981).
66. Hyder, C.L., Pallari, H.-M., Kochin, V. and Eriksson, J.E. Providing cellular signposts – Post-translational modifications of intermediate filaments. FEBS Lett 582, 2140-2148 (2008).
67. Tsujimura, K., Ogawara, M., Takeuchi, Y., Imajoh-Ohmi, S., Ha, M.H. and Inagaki, M. Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J Biol Chem 269, 31097-31106 (1994).
68. Geisler, N., Hatzfeld, M. and Weber, K. Phosphorylation in vitro of vimentin by protein kinases A and C is restricted to the head domain. Identification of the phosphoserine sites and their influence on filament formation. Eur J Biochem 183, 441-447 (1989).
69. Ando, S., Tanabe, K., Gonda, Y., Sato, C. and Inagaki, M. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28, 2974-2979 (1989).
70. Lee, D.Y., Teyssier, C., Strahl, B.D. and Stallcup, M.R. Role of protein methylation in regulation of transcription. Endocr Rev 26, 147-170 (2005).
71. Lee, Y.H. and Stallcup, M.R. Minireview: Protein Arginine Methylation of Nonhistone Proteins in Transcriptional Regulation. Molecular Endocrinology 23, 425-433 (2009).
72. Bedford, M.T. and Clarke, S.G. Protein Arginine Methylation in Mammals: Who, What, and Why. Mol Cell 33, 1-13 (2009).
73. McBride, A.E. and Silver, P.A. State of the arg: protein methylation at arginine comes of age. Cell 106, 5-8 (2001).
74. Tang, J., Frankel, A., Cook, R.J., Kim, S., Paik, W.K., Williams, K.R., et al. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J Biol Chem 275, 7723-7730 (2000).
75. Bedford, M.T. and Richard, S. Arginine MethylationAn Emerging Regulatorof Protein Function. Mol Cell 18, 263-272 (2005).
76. Huang, S., Litt, M. and Felsenfeld, G. Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications. Genes Dev 19, 1885-1893 (2005).
77. Zhang, X. and Cheng, X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 11, 509-520 (2003).
78. Gary, J.D. and Clarke, S. RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acid Res Mol Biol 61, 65-131 (1998).
79. Smith, J.J., Rucknagel, K.P., Schierhorn, A., Tang, J., Nemeth, A., Linder, M., et al. Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J Biol Chem 274, 13229-13234 (1999).
80. Klein, S., Carroll, J.A., Chen, Y., Henry, M.F., Henry, P.A., Ortonowski, I.E., et al. Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2. J Biol Chem 275, 3150-3157 (2000).
81. Tang, J., Kao, P.N. and Herschman, H.R. Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. J Biol Chem 275, 19866-19876 (2000).
82. Kwak, Y.T., Guo, J., Prajapati, S., Park, K.J., Surabhi, R.M., Miller, B., et al. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell 11, 1055-1066 (2003).
83. Boisvert, F.M., Rhie, A., Richard, S. and Doherty, A.J. The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell Cycle 4, 1834-1841 (2005).
84. Ostareck-Lederer, A., Ostareck, D.H., Rucknagel, K.P., Schierhorn, A., Moritz, B., Huttelmaier, S., et al. Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src. J Biol Chem 281, 11115-11125 (2006).
85. Yamagata, K., Daitoku, H., Takahashi, Y., Namiki, K., Hisatake, K., Kako, K., et al. Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt. Mol Cell 32, 221-231 (2008).
86. Chang, Y.-I., Lin, S.-W., Chiou, Y.-Y., Sung, J.-S., Cheng, L.-C., Lu, Y.-L., et al. Establishment of an ectopically expressed and functional PRMT1 for proteomic analysis of arginine-methylated proteins. Electrophoresis 31, 3834-3842 (2010).
87. Siebert, P.D. and Fukuda, M. Induction of cytoskeletal vimentin and actin gene expression by a tumor-promoting phorbol ester in the human leukemic cell line K562. J Biol Chem 260, 3868-3874 (1985).
88. Vazquez-Martin, A., Oliveras-Ferraros, C., Colomer, R., Brunet, J. and Menendez, J.A. Low-scale phosphoproteome analyses identify the mTOR effector p70 S6 kinase 1 as a specific biomarker of the dual-HER1/HER2 tyrosine kinase inhibitor lapatinib (Tykerb) in human breast carcinoma cells. Ann Oncol 19, 1097-1109 (2008).
89. Hsu, J.M., Chen, C.T., Chou, C.K., Kuo, H.P., Li, L.Y., Lin, C.Y., et al. Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation. Nat Cell Biol 13, 174-181 (2011).
90. Bobick, B.E., Tuan, R.S. and Chen, F.H. The intermediate filament vimentin regulates chondrogenesis of adult human bone marrow-derived multipotent progenitor cells. J Cell Biochem 109, 265-276 (2010).
91. Mendez, M.G., Kojima, S. and Goldman, R.D. Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition. FASEB J 24, 1838-1851 (2010).
92. Styers, M.L., Salazar, G., Love, R., Peden, A.A., Kowalczyk, A.P. and Faundez, V. The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton. Mol Biol Cell 15, 5369-5382 (2004).
93. Parsons, M., Keppler, M.D., Kline, A., Messent, A., Humphries, M.J., Gilchrist, R., et al. Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis. Mol Cell Biol 22, 5897-5911 (2002).
94. Holen, I., Gordon, P.B. and Seglen, P.O. Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity. Biochem J 284 ( Pt 3), 633-636 (1992).
95. Kumar, N., Robidoux, J., Daniel, K.W., Guzman, G., Floering, L.M. and Collins, S. Requirement of vimentin filament assembly for beta3-adrenergic receptor activation of ERK MAP kinase and lipolysis. J Biol Chem 282, 9244-9250 (2007).
96. Robidoux, J., Kumar, N., Daniel, K.W., Moukdar, F., Cyr, M., Medvedev, A.V., et al. Maximal beta3-adrenergic regulation of lipolysis involves Src and epidermal growth factor receptor-dependent ERK1/2 activation. J Biol Chem 281, 37794-37802 (2006).
97. Sin, W.C., Chen, X.Q., Leung, T. and Lim, L. RhoA-binding kinase alpha translocation is facilitated by the collapse of the vimentin intermediate filament network. Mol Cell Biol 18, 6325-6339 (1998).
98. Eriksson, J.E., Brautigan, D.L., Vallee, R., Olmsted, J., Fujiki, H. and Goldman, R.D. Cytoskeletal integrity in interphase cells requires protein phosphatase activity. Proc Natl Acad Sci U S A 89, 11093-11097 (1992).
99. Eriksson, J.E., He, T., Trejo-Skalli, A.V., Harmala-Brasken, A.S., Hellman, J., Chou, Y.H., et al. Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments. J Cell Sci 117, 919-932 (2004).
100. Kochin, V., Imanishi, S.Y. and Eriksson, J.E. Fast track to a phosphoprotein sketch - MALDI-TOF characterization of TLC-based tryptic phosphopeptide maps at femtomolar detection sensitivity. Proteomics 6, 5676-5682 (2006).
101. Chou, Y.H., Bischoff, J.R., Beach, D. and Goldman, R.D. Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin. Cell 62, 1063-1071 (1990).
102. Chou, Y.H., Ngai, K.L. and Goldman, R. The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site. J Biol Chem 266, 7325-7328 (1991).
103. Goto, H., Kosako, H., Tanabe, K., Yanagida, M., Sakurai, M., Amano, M., et al. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J Biol Chem 273, 11728-11736 (1998).
104. Goto, H., Yasui, Y., Kawajiri, A., Nigg, E.A., Terada, Y., Tatsuka, M., et al. Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J Biol Chem 278, 8526-8530 (2003).
105. Takai, Y., Ogawara, M., Tomono, Y., Moritoh, C., Imajoh-Ohmi, S., Tsutsumi, O., et al. Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. J Cell Biol 133, 141-149 (1996).
106. Yamaguchi, T., Goto, H., Yokoyama, T., Sillje, H., Hanisch, A., Uldschmid, A., et al. Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. J Cell Biol 171, 431-436 (2005).
107. Stefanovic, S., Windsor, M., Nagata, K.I., Inagaki, M. and 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 79, 11766-11775 (2005).
108. Omary, M.B., Ku, N.O., Tao, G.Z., Toivola, D.M. and Liao, J. "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem Sci 31, 383-394 (2006).
|