Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 34, 2012, Pages 13620-13625

  Chernyatina, Anastasia A ^a   Nicolet, Stefan ^a   Aebi, Ueli ^b   Herrmann, Harald ^c   Strelkov, Sergei V ^a  

^a DEPARTMENT OF PHARMACEUTICAL AND PHARMACOLOGICAL SCIENCES   (Belgium)

^b UNIVERSITY OF BASEL   (Switzerland)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

Coiled coil; Cytoskeleton; X ray crystallography

Indexed keywords

TETRAMER; VIMENTIN;

ALPHA HELIX; ARTICLE; CRYSTAL STRUCTURE; INTERMEDIATE FILAMENT; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ANALYSIS; SURFACE CHARGE; TANDEM REPEAT;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; CYTOSKELETON; DIMERIZATION; ESCHERICHIA COLI; HUMANS; INTERMEDIATE FILAMENTS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; VIMENTIN;

EID: 84865305368     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1206836109     Document Type: Article

References (42)

1. Fuchs E, Weber K (1994) Intermediate filaments: Structure, dynamics, function, and disease. Annu Rev Biochem 63:345-382.
2. Herrmann H, Bar H, Kreplak L, Strelkov SV, Aebi U (2007) Intermediate filaments: From cell architecture to nanomechanics. Nat Rev Mol Cell Biol 8:562-573.
3. Lazarides E (1982) Intermediate filaments: A chemically heterogeneous, developmentally regulated class of proteins. Annu Rev Biochem 51:219-250.
4. Herrmann H, Hesse M, Reichenzeller M, Aebi U, Magin TM (2003) Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation. Int Rev Cytol 223:83-175.
5. Herrmann H, Aebi U (2004) Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu Rev Biochem 73:749-789.
6. Parry DA (1982) Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiledcoils in other proteins. Biosci Rep 2:1017-1024.
7. Herrmann H, et al. (1996) Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod, and tail domains. J Mol Biol 264:933-953.
8. Lichtenstern T, Mucke N, Aebi U, Mauermann M, Herrmann H (2012) Complex formation and kinetics of filament assembly exhibited by the simple epithelial keratins K8 and K18. J Struct Biol 177:54-62.
9. Steinert PM, Marekov LN, Fraser RD, Parry DA (1993) Keratin intermediate filament structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J Mol Biol 230:436-452.
10. Steinert PM, Marekov LN, Parry DA (1993) 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.
11. Hess JF, Budamagunta MS, Voss JC, FitzGerald PG (2004) Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using SDSL and EPR. J Biol Chem 279:44841-44846.
12. Mucke N, et al. (2004) Molecular and biophysical characterization of assembly-starter units of human vimentin. J Mol Biol 340:97-114.
13. Quax-Jeuken YE, Quax WJ, Bloemendal H (1983) Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc Natl Acad Sci USA 80:3548-3552.
14. Strelkov SV, Herrmann H, Aebi U (2003) Molecular architecture of intermediate filaments. Bioessays 25:243-251.
15. Parry DAD, Steinert PM (1999) Intermediate filaments: Molecular architecture, assembly, dynamics, and polymorphism. Q Rev Biophys 32:99-187.
16. Omary MB (2009) "IF-pathies": A broad spectrum of intermediate filament-associated diseases. J Clin Invest 119:1756-1762.
17. Strelkov SV, et al. (2001) Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J Mol Biol 306:773-781.
18. Strelkov SV, et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly. EMBO J 21:1255-1266.
19. Nicolet S, Herrmann H, Aebi U, Strelkov SV (2010) Atomic structure of vimentin coil 2. J Struct Biol 170:369-376.
20. Chernyatina AA, Strelkov SV (2012) Stabilization of vimentin coil-2 fragment via an engineered disulfide. J Struct Biol 177:46-53.
21. Dhe-Paganon S,Werner ED, Chi YI, Shoelson SE (2002) Structure of the globular tail of nuclear lamin. J Biol Chem 277:17381-17384.
22. Cole C, Barber JD, Barton GJ (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36:W197-W201.
23. Petersen B, Petersen TN, Andersen P, Nielsen M, Lundegaard C (2009) A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct Biol 9:51.
24. Lupas A (1997) Predicting coiled-coil regions in proteins. Curr Opin Struct Biol 7:388-393.
25. Gruber M, Lupas AN (2003) Historical review: Another 50th anniversary-new periodicities in coiled coils. Trends Biochem Sci 28:679-685.
26. Kuhnel K, et al. (2004) The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proc Natl Acad Sci USA 101:17027-17032.
27. Meier M, et al. (2009) Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation. J Mol Biol 390:245-261.
28. Brown JH, Cohen C, Parry DA (1996) Heptad breaks in alpha-helical coiled coils: Stutters and stammers. Proteins 26:134-145.
29. Smith TA, Strelkov SV, Burkhard P, Aebi U, Parry DA (2002) Sequence comparisons of intermediate filament chains: Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. J Struct Biol 137:128-145.
30. Parry DA, Smith TA (2010) A different conformation for linker L12 in IF molecules in the molecular and filamentous forms: An hypothesis. J Struct Biol 170:364-368.
31. Parry DA, Crewther WG, Fraser RD, MacRae TP (1977) 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.
32. McLachlan AD, Stewart M (1982) Periodic charge distribution in the intermediate filament proteins desmin and vimentin. J Mol Biol 162:693-698.
33. Georgakopoulou S, Moller D, Sachs N, Herrmann H, Aebi U (2009) Near-UV circular dichroism reveals structural transitions of vimentin subunits during intermediate filament assembly. J Mol Biol 386:544-553.
34. Smith TA, Strelkov SV, Burkhard P, Aebi U, Parry DA (2002) Sequence comparisons of intermediate filament chains: Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. J Struct Biol 137:128-145.
35. Aziz A, Hess JF, Budamagunta MS, FitzGerald PG, Voss JC (2009) Head and rod 1 interactions in vimentin: Identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance. J Biol Chem 284:7330-7338.
36. Schaffeld M, Herrmann H, Schultess J, Markl J (2001) Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns, and in vitro assembly. Eur J Cell Biol 80:692-702.
37. Barlow DJ, Thornton JM (1988) Helix geometry in proteins. J Mol Biol 201:601-619.
38. Strelkov SV, Kreplak L, Herrmann H, Aebi U (2004) Intermediate filament protein structure determination. Methods Cell Biol 78:25-43.
39. Weeks SD, Drinker M, Loll PJ (2007) Ligation independent cloning vectors for expression of SUMO fusions. Protein Expr Purif 53:40-50.
40. DeLano WL (2002) The PyMOL User's Manual (DeLano Scientific, San Carlos, CA).
41. Strelkov SV, Burkhard P (2002) Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J Struct Biol 137:54-64.
42. Chernyatina AA, Strelkov SV (2012) Stabilization of vimentin coil-2 fragment via an engineered disulfide. J Struct Biol 177:46-53.