Abstract
Profilin is an actin monomer-binding protein which stimulates actin polymerization. Recent studies have revealed that profilin interacts with VASP, Mena, Bnilp, Bnrlp, and mDia, all of which have the proline-rich domain. Here, we isolated three profilin-binding proteins from rat brain cytosol by glutathione S-transferase-profilin affinity column chromatography and identified them as Mena, drebrin, and gephyrin. These proteins had a proline-rich domain and directly interacted with profilin.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Binding Sites / genetics
-
Brain / metabolism
-
Carrier Proteins / genetics
-
Carrier Proteins / isolation & purification
-
Carrier Proteins / metabolism*
-
Contractile Proteins*
-
Cytosol / metabolism
-
Humans
-
In Vitro Techniques
-
Membrane Proteins / genetics
-
Membrane Proteins / isolation & purification
-
Membrane Proteins / metabolism*
-
Microfilament Proteins / metabolism*
-
Molecular Sequence Data
-
Neuropeptides / genetics
-
Neuropeptides / isolation & purification
-
Neuropeptides / metabolism*
-
Peptide Mapping
-
Profilins
-
Proline / chemistry
-
Protein Binding
-
Rats
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / isolation & purification
-
Recombinant Fusion Proteins / metabolism
Substances
-
Carrier Proteins
-
Contractile Proteins
-
Membrane Proteins
-
Microfilament Proteins
-
Neuropeptides
-
PFN1 protein, human
-
Pfn1 protein, rat
-
Profilins
-
Recombinant Fusion Proteins
-
drebrins
-
gephyrin
-
Proline