Cleavage of the Intermediate Filament Subunit Protein Vimentin by HIV-1 Protease: Utilization of a Novel Cleavage Site and Identification of Higher Order Polymers of Pepstatin A
Intermediate filaments (IFs) are important constituents of the eukaryotic cell cytoskeleton. They are 10-12 nm in diameter and are composed of one or more of over 40 different subunit proteins, belonging to 5 classes of cytoplasmic and 1 class of nuclear proteins (the lamins). These proteins all possess a central rod domain, with a highly conserved amino acid sequence, which allow the IF proteins to form dimers through coiled coil interactions (much like myosin). These dimers, in turn, can polymerize into higher order structures which culminate in the final 10 nm filaments. As reviewed by Traub (1985) and Steinert and Roop (1988), much is known about the physical chemistry, molecular biology and tissue specific distribution of IF proteins; disappointingly little is known about their cellular functions. In addition to their role as cytoskeletal elements, it has been proposed that IF proteins may also participate in regulating expression of genetic information (Traub et al., 1987; Chan et al., 1989), although definitive proof of this role is still lacking.
KeywordsHuman Immunodeficiency Virus Type Intermediate Filament Equine Infectious Anemia Virus Conserve Amino Acid Sequence Tail Domain
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