Abstract
We studied the molecular associations between peripherin (a neuronal, type III intermediate filament subunit) and nuclear lamins. We show here that isolated peripherin binds selectively to mammalian lamin B under in vitro conditions. We further demonstrate that a synthetic peptide, representing the proximal part of peripherin's tail domain (P1), also associates with mammalian lamin B in a saturable, cooperative, and specific fashion. Laboratory animals immunized with P1 spontaneously develop idiotypic and anti-idiotypic antibodies recognizing peripherin and lamin B, respectively. These data provide essentially in vivo evidence that lamin B represents a constitutive nuclear "receptor" site for the tail domains of peripherin intermediate filaments.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Cell Line
-
Cell Nucleus / physiology
-
Cell Nucleus / ultrastructure*
-
Cells, Cultured
-
Embryo, Mammalian
-
Embryo, Nonmammalian
-
Erythrocytes / physiology
-
Erythrocytes / ultrastructure*
-
Fluorescent Antibody Technique
-
Immunoblotting
-
Intermediate Filament Proteins / genetics
-
Intermediate Filament Proteins / metabolism*
-
Intermediate Filaments / physiology
-
Intermediate Filaments / ultrastructure*
-
Kinetics
-
Lamin Type B
-
Lamins
-
Membrane Glycoproteins*
-
Mice
-
Microsomes, Liver / physiology
-
Microsomes, Liver / ultrastructure*
-
Mitochondria, Liver / physiology
-
Mitochondria, Liver / ultrastructure*
-
Molecular Sequence Data
-
Nerve Tissue Proteins*
-
Neuroblastoma
-
Neurons / physiology
-
Neurons / ultrastructure*
-
Neuropeptides / metabolism
-
Nuclear Proteins / metabolism*
-
Peripherins
-
Protein Binding
-
Rats
-
Restriction Mapping
-
Turkeys
Substances
-
Intermediate Filament Proteins
-
Lamin Type B
-
Lamins
-
Membrane Glycoproteins
-
Nerve Tissue Proteins
-
Neuropeptides
-
Nuclear Proteins
-
Peripherins