Vimentin's tail interacts with actin-containing structures in vivo

The tail domain of the intermediate filament (IF) protein vimentin is unnecessary for IF assembly in vitro. To study the role of vimentin's tail in vivo, we constructed a plasmid that directs the synthesis of a 'myc-tagged' version of the Xenopus vimentin-1 tail domain in bacteria. Th...

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Veröffentlicht in:	Journal of cell science 1994-06, Vol.107 (6), p.1609-1622
Hauptverfasser:	CARY, R. B, KLYMKOWSKY, M. W, EVANS, R. M, DOMINGO, A, DENT, J. A, BACKHUS, L. E
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding Sites Biological and medical sciences Cells, Cultured Chemical Phenomena Chemistry, Physical Contractile proteins Cytochalasin B - pharmacology Fundamental and applied biological sciences. Psychology Genes, myc Holoproteins Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Secondary Proteins Recombinant Fusion Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Vimentin - chemistry Vimentin - metabolism Xenopus
Online-Zugang:	Volltext
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