Structural and functional differences between KRIT1A and KRIT1B isoforms: A framework for understanding CCM pathogenesis(525 views) Francalanci F, Avolio M, De Luca E, Longo DL, Menchise V, Guazzi P, Sgro F, Marino M, Goitre L, Balzac F, Trabalzini L, Retta SF
Exp Cell Res (ISSN: 0014-4827), 2009 Jan 15; 315(2): 285-303.
Keywords: Ccm, Ferm Domain, Head-To-Tail Protein Interaction, Homology Modeling, Icap1, Krit1, Ligand Docking, Nucleocytoplasmic Shuttling, Rap1a, Yeast Two-Hybrid Interaction, Cell Protein, Protein Krit1a, Rap1 Protein, Rap1a Protein, Unclassified Drug, Animal Cell, Article, Brain Malformation, Cellular Distribution, Cerebral Cavernous Malformation, Controlled Study, Exon, Molecular Model, Nonhuman, Nucleotide Sequence, Pathogenesis, Priority Journal, Protein Binding, Protein Domain, Protein Localization, Protein Protein Interaction, Protein Structure, Protein Transport, Sequence Homology, Structure Activity Relation, Cell Line, Central Nervous System Vascular Malformations, Cercopithecus Aethiops, Computer Simulation, Cos Cells, Hela Cells, Hemangioma, Intracellular Signaling Peptides And Proteins, Microfilament Proteins, Microtubule-Associated Proteins, Peptide Fragments, Point Mutation, Protein Interaction Domains And Motifs, Protein Isoforms, Secondary, Proto-Oncogene Proteins, Rap1 Gtp-Binding Proteins, Recombinant Fusion Proteins, Two-Hybrid System Techniques,
Affiliations: *** IBB - CNR ***
Molecular Biotechnology Centre, Department of Genetics, Biology and Biochemistry, Via Nizza 52, 10126 Torino, Italy
Department of Molecular Biology, University of Siena, Italy
Department of Chemistry IFM, University of Torino, Italy
Institute of Biostructure and Bioimaging, National Research Council of Napoli, Italy
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Retta, S. F., Balzac, F., Avolio, M., Rap1: a turnabout for the crosstalk between cadherins and integrins (2006) Eur. J. Cell Biol., 85, pp. 283-293
Pearson, M. A., Reczek, D., Bretscher, A., Karplus, P. A., Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain (2000) Cell, 101, pp. 259-270
Ceccarelli, D. F., Song, H. K., Poy, F., Schaller, M. D., Eck, M. J., Crystal structure of the FERM domain of focal adhesion kinase (2006) J. Biol. Chem., 281, pp. 252-259
Han, B. G., Nunomura, W., Wu, H., Mohandas, N., Jap, B. K., Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4. 1 from human erythrocytes (2000) Acta Crystallogr. D. Biol. Crystallogr., 56, pp. 187-188
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Retta, S. F., Avolio, M., Francalanci, F., Procida, S., Balzac, F., Degani, S., Tarone, G., Silengo, L., Identification of Krit1B: a novel alternative splicing isoform of cerebral cavernous malformation gene-1 (2004) Gene, 325, pp. 63-78
Thompson, J. D., Higgins, D. G., Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22, pp. 4673-4680
Kang, B. S., Cooper, D. R., Devedjiev, Y., Derewenda, U., Derewenda, Z. S., The structure of the FERM domain of merlin, the neurofibromatosis type 2 gene product (2002) Acta Crystallogr. D. Biol. Crystallogr., 58, pp. 381-391
Sippl, M. J., Recognition of errors in three-dimensional structures of proteins (1993) Proteins, 17, pp. 355-362
Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., Errors in protein structures (1996) Nature, 381, p. 272
Cornell, W. D., Cieplak, P., Bayly, C. I., Gould, I. R., Merz, K. M., Ferguson, D. M., Spellmeyer, D. C., Kollman, P. A., A second-generation force field for the simulation of proteins, nucleic acids, and organic molecules (1995) J. Am. Chem. Soc., 117, pp. 5179-5197
Halgren, T. A., Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94 (1996) J. Comput. Chem., 17, pp. 490-519
Toby, G. G., Golemis, E. A., Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions (2001) Methods, 24, pp. 201-217
Kelley, L. A., MacCallum, R. M., Sternberg, M. J., Enhanced genome annotation using structural profiles in the program 3D-PSSM (2000) J. Mol. Biol., 299, pp. 499-520
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Uhlik, M. T., Temple, B., Bencharit, S., Kimple, A. J., Siderovski, D. P., Johnson, G. L., Structural and evolutionary division of phosphotyrosine binding (PTB) domains (2005) J. Mol. Biol., 345, pp. 1-20
Yan, K. S., Kuti, M., Zhou, M. M., PTB or not PTB-that is the question (2002) FEBS Lett., 513, pp. 67-70
Campbell, S. J., Gold, N. D., Jackson, R. M., Westhead, D. R., Ligand binding: functional site location, similarity and docking (2003) Curr. Opin. Struct. Biol., 13, pp. 389-395
Calderwood, D. A., Fujioka, Y., de Pereda, J. M., Garcia-Alvarez, B., Nakamoto, T., Margolis, B., McGlade, C. J., Ginsberg, M. H., Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 2272-2277
Pufall, M. A., Graves, B. J., Autoinhibitory domains: modular effectors of cellular regulation (2002) Annu. Rev. Cell Dev. Biol., 18, pp. 421-462
Li, Q., Nance, M. R., Kulikauskas, R., Nyberg, K., Fehon, R., Karplus, P. A., Bretscher, A., Tesmer, J. J., Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain (2007) J. Mol. Biol., 365, pp. 1446-1459
Luque, C. M., Correas, I., A constitutive region is responsible for nuclear targeting of 4. 1R: modulation by alternative sequences results in differential intracellular localization (2000) J. Cell Sci., 113 (PART 13), pp. 2485-2495
Structural and functional differences between KRIT1A and KRIT1B isoforms: A framework for understanding CCM pathogenesis