HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Steinert, P. M. Articles by Parry, D. A. D. Search for Related Content PubMed PubMed Citation Articles by Steinert, P. M. Articles by Parry, D. A. D. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 3, 1657-1666, January 15, 1999

Molecular Parameters of Type IV -Internexin and Type IV-Type III -Internexin-Vimentin Copolymer Intermediate Filaments

Peter M. Steinert, Lyuben N. Marekov, and David A. D. Parry^¶

From the  Laboratory of Skin Biology, NIAMS, National Institutes of Health, Bethesda, Maryland 20892-2752 and ^¶ Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand

During neuronal development, a dynamic replacement mechanism occurs in which the type VI nestin and type III vimentin intermediate filament proteins are replaced by a series of type IV proteins beginning with -internexin. We have explored molecular details of how the type III to type IV replacement process may occur. First, we have demonstrated by cross-linking experiments that bacterially expressed forms of -internexin and vimentin form heterodimer molecules in vitro that assemble into copolymer intermediate filaments. We show using a urea disassembly assay that -internexin molecules are likely to be more stable than those of vimentin. Second, by analyses of the induced cross-links, we have determined the axial lengths of -internexin homodimer and -internexin-vimentin heterodimer molecules and their modes of alignments in filaments. We report that these dimensions are the same as those reported earlier for vimentin homopolymer molecules and, by implication, are also the same for the other neuronal type IV proteins. These data suggest that during neuronal development, -internexin molecules are readily assimilated onto the pre-existing vimentin cytoskeletal intermediate filament network because the axial lengths and axial alignments of their molecules are the same. Furthermore, the dynamic replacement process may be driven by a positive equilibrium due to the increased stability of the -internexin network.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Yuan, M. V. Rao, T. Sasaki, Y. Chen, A. Kumar, Veeranna, R. K. H. Liem, J. Eyer, A. C. Peterson, J.-P. Julien, et al. {alpha}-Internexin Is Structurally and Functionally Associated with the Neurofilament Triplet Proteins in the Mature CNS J. Neurosci., September 27, 2006; 26(39): 10006 - 10019. [Abstract] [Full Text] [PDF]

				V. C. Hsiao, R. Tian, H. Long, M. Der Perng, M. Brenner, R. A. Quinlan, and J. E. Goldman Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP J. Cell Sci., May 1, 2005; 118(9): 2057 - 2065. [Abstract] [Full Text] [PDF]

				G. T. Park, S. E. Lim, S.-I. Jang, and M. I. Morasso Suprabasin, a Novel Epidermal Differentiation Marker and Potential Cornified Envelope Precursor J. Biol. Chem., November 15, 2002; 277(47): 45195 - 45202. [Abstract] [Full Text] [PDF]

				D. A. D. Parry, L. N. Marekov, and P. M. Steinert Subfilamentous Protofibril Structures in Fibrous Proteins. CROSS-LINKING EVIDENCE FOR PROTOFIBRILS IN INTERMEDIATE FILAMENTS J. Biol. Chem., October 12, 2001; 276(42): 39253 - 39258. [Abstract] [Full Text] [PDF]

				H. Wang, D. A.D. Parry, L. N. Jones, W. W. Idler, L. N. Marekov, and P. M. Steinert In Vitro Assembly and Structure of Trichocyte Keratin Intermediate Filaments: A Novel Role for Stabilization by Disulfide Bonding J. Cell Biol., December 27, 2000; 151(7): 1459 - 1468. [Abstract] [Full Text] [PDF]

				K. C. Wu, J. T. Bryan, M. I. Morasso, S.-I. Jang, J.-H. Lee, J.-M. Yang, L. N. Marekov, D. A.D. Parry, and P. M. Steinert Coiled-Coil Trigger Motifs in the 1B and 2B Rod Domain Segments Are Required for the Stability of Keratin Intermediate Filaments Mol. Biol. Cell, October 1, 2000; 11(10): 3539 - 3558. [Abstract] [Full Text]

				P. M. Steinert, Y.-H. Chou, V. Prahlad, D. A. D. Parry, L. N. Marekov, K. C. Wu, S.-I. Jang, and R. D. Goldman A High Molecular Weight Intermediate Filament-associated Protein in BHK-21 Cells Is Nestin, a Type VI Intermediate Filament Protein. LIMITED CO-ASSEMBLY IN VITRO TO FORM HETEROPOLYMERS WITH TYPE III VIMENTIN AND TYPE IV alpha -INTERNEXIN J. Biol. Chem., April 2, 1999; 274(14): 9881 - 9890. [Abstract] [Full Text] [PDF]

				T. Mehrani, K. C. Wu, M. I. Morasso, J. T. Bryan, L. N. Marekov, D. A. D. Parry, and P. M. Steinert Residues in the 1A Rod Domain Segment and the Linker L2 Are Required for Stabilizing the A11 Molecular Alignment Mode in Keratin Intermediate Filaments J. Biol. Chem., January 12, 2001; 276(3): 2088 - 2097. [Abstract] [Full Text] [PDF]