The Structure of a Tandem Pair of Spectrin Repeats of Plectin Reveals a Modular Organization of the Plakin Domain

Journal of Molecular Biology

Volumn 368, Issue 5, 2007, Pages 1379-1391

  Sonnenberg, Arnoud ^a   Rojas, Ana M ^b   de Pereda, José M ^c  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

^b Centro Nacional de Investigaciones Oncológicas   (Spain)

^c UNIVERSITY OF SALAMANCA   (Spain)

Author keywords

cytoskeleton; epithelium; hemidesmosome; X ray crystallography

Indexed keywords

ACTIN; INTEGRIN; PLAKIN; PLECTIN; PROTEIN SH3; SPECTRIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CANONICAL ANALYSIS; GENE INSERTION; HEMIDESMOSOME; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN STRUCTURE;

EID: 34247222123     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.090     Document Type: Article

References (57)

1. Wiche G. Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 111 (1998) 2477-2486
2. Jefferson J.J., Leung C.L., and Liem R.K. Plakins: goliaths that link cell junctions and the cytoskeleton. Nature Rev. Mol. Cell. Biol. 5 (2004) 542-553
3. Wiche G., Krepler R., Artlieb U., Pytela R., and Aberer W. Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp. Cell Res. 155 (1984) 43-49
4. Hieda Y., Nishizawa Y., Uematsu J., and Owaribe K. Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116 (1992) 1497-1506
5. Litjens S.H., de Pereda J.M., and Sonnenberg A. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 16 (2006) 376-383
6. Rezniczek G.A., de Pereda J.M., Reipert S., and Wiche G. Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites. J. Cell Biol. 141 (1998) 209-225
7. Geerts D., Fontao L., Nievers M.G., Schaapveld R.Q., Purkis P.E., Wheeler G.N., et al. Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147 (1999) 417-434
8. Koster J., van Wilpe S., Kuikman I., Litjens S.H., and Sonnenberg A. Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes. Mol. Biol. Cell 15 (2004) 1211-1223
9. Koster J., Geerts D., Favre B., Borradori L., and Sonnenberg A. Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly. J. Cell Sci. 116 (2003) 387-399
10. Nikolic B., Mac Nulty E., Mir B., and Wiche G. Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J. Cell Biol. 134 (1996) 1455-1467
11. Steinbock F.A., Nikolic B., Coulombe P.A., Fuchs E., Traub P., and Wiche G. Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain. J. Cell Sci. 113 (2000) 483-491
12. Pfendner E., Rouan F., and Uitto J. Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations. Exp. Dermatol. 14 (2005) 241-249
13. Andra K., Lassmann H., Bittner R., Shorny S., Fassler R., Propst F., and Wiche G. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 11 (1997) 3143-3156
14. Green K.J., Virata M.L., Elgart G.W., Stanley J.R., and Parry D.A. Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments. Int. J. Biol. Macromol. 14 (1992) 145-153
15. Jefferson J.J., Ciatto C., Shapiro L., and Liem R.K. Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily. J. Mol. Biol. 336 (2007) 244-257
16. Kleywegt G.J., and Jones T.A. Phi/psi-chology: ramachandran revisited. Structure 4 (1996) 1395-1400
17. Cruickshank D.W. Remarks about protein structure precision. Acta Crystallog. sect. D 55 (1999) 583-601
18. Lupas A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21 (1996) 375-382
19. Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
20. Djinovic-Carugo K., Young P., Gautel M., and Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 98 (1999) 537-546
21. Grum V.L., Li D., MacDonald R.I., and Mondragon A. Structures of two repeats of spectrin suggest models of flexibility. Cell 98 (1999) 523-535
22. Kusunoki H., MacDonald R.I., and Mondragon A. Structural insights into the stability and flexibility of unusual erythroid spectrin repeats. Structure 12 (2004) 645-656
23. Park S., Caffrey M.S., Johnson M.E., and Fung L.W. Solution structural studies on human erythrocyte alpha-spectrin tetramerization site. J. Biol. Chem. 278 (2003) 21837-21844
24. Ylanne J., Scheffzek K., Young P., and Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure 9 (2001) 597-604
25. Kusunoki H., Minasov G., Macdonald R.I., and Mondragon A. Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin. J. Mol. Biol. 344 (2004) 495-511
26. Eddy S.R. Profile hidden Markov models. Bioinformatics 14 (1998) 755-763
27. Rychlewski L., Jaroszewski L., Li W., and Godzik A. Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci. 9 (2000) 232-241
28. Pascual J., Castresana J., and Saraste M. Evolution of the spectrin repeat. Bioessays 19 (1997) 811-817
29. Garcia-Alvarez B., Bobkov A., Sonnenberg A., and de Pereda J.M. Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and to integrin a6b4. Structure 11 (2003) 615-625
30. Andreotti A.H., Bunnell S.C., Feng S., Berg L.J., and Schreiber S.L. Regulatory intramolecular association in a tyrosine kinase of the Tec family. Nature 385 (1997) 93-97
31. Pursglove S.E., Mulhern T.D., Mackay J.P., Hinds M.G., and Booker G.W. The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain. J. Biol. Chem. 277 (2002) 755-762
32. Leung C.L., Zheng M., Prater S.M., and Liem R.K. The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles. J. Cell Biol. 154 (2001) 691-697
33. Pascual J., Castresana J., and Saraste M. Evolution of the spectrin repeat. Bioessays 19 (1997) 811-817
34. Foisner R., and Wiche G. Structure and hydrodynamic properties of plectin molecules. J. Mol. Biol. 198 (1987) 515-531
35. Svitkina T.M., Verkhovsky A.B., and Borisy G.G. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Cell Biol. 135 (1996) 991-1007
36. Broderick M.J., and Winder S.J. Spectrin, alpha-actinin, and dystrophin. Advan. Protein Chem. 70 (2005) 203-246
37. Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R., and Liddington R.C. Crystal structure of the vinculin tail suggests a pathway for activation. Cell 99 (1999) 603-613
38. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
39. Sheldrick G.M. Macromolecular phasing with SHELXE. Z. Kristallog. 217 (2002) 644-650
40. Sheldrick G.M., and Schneider T.R. SHELXL: high resolution refinement. Methods Enzymol. 277 (1997) 319-343
41. Pape T., and Schneider T.R. HKL2MAP: a graphical user interface for phasing with SHELX programs. J. Appl. Crystallog. 37 (2004) 843-844
42. Cowtan K. 'dm': an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsletter Protein Crystallog. 31 (1994) 34-38
43. Morris R.J., Zwart P.H., Cohen S., Fernandez F.J., Kakaris M., Kirillova O., et al. Breaking good resolutions with ARP/wARP. Synchrotron Radiat. 11 (2004) 56-59
44. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
45. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
46. Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallog. sect. D 62 (2006) 439-450
47. Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
48. Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A 32 (1976) 922-923
49. Collaborative Computational Project, Number 4. The CCP4 Suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
50. Barrett C.P., Hall B.A., and Noble M.E. Dynamite: a simple way to gain insight into protein motions. Acta Crystallog. sect. D 60 (2004) 2280-2287
51. de Groot B.L., van Aalten D.M., Scheek R.M., Amadei A., Vriend G., and Berendsen H.J. Prediction of protein conformational freedom from distance constraints. Proteins: Struct. Funct. Genet. 29 (1997) 240-251
52. Van Der Spoel D., Lindahl E., Hess B., Groenhof G., Mark A.E., and Berendsen H.J. ROMACS: fast, flexible, and free. J. Comput. Chem. 26 (2005) 1701-1718
53. Letunic I., Copley R.R., Pils B., Pinkert S., Schultz J., and Bork P. SMART 5: domains in the context of genomes and networks. Nucl. Acids Res. 34 (2006) D257-D260
54. Finn R.D., Mistry J., Schuster-Bockler B., Griffiths-Jones S., Hollich V., Lassmann T., et al. Pfam: clans, web tools and services. Nucl. Acids Res. 34 (2006) D247-D251
55. Rost B., Yachdav G., and Liu J. The PredictProtein server. Nucl. Acids Res. 32 (2004) W321-W326
56. DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, San Carlos, CA, USA
57. Diederichs K., and Karplus P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nature Struct. Biol. 4 (1997) 269-275