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Interactions of drebrin and gephyrin with profilin. Biochem Biophys Res Commun 1998 Feb 04;243(1):86-9

Date

02/25/1998

Pubmed ID

9473484

DOI

10.1006/bbrc.1997.8068

Scopus ID

2-s2.0-0032481298 (requires institutional sign-in at Scopus site)   126 Citations

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.

Author List

Mammoto A, Sasaki T, Asakura T, Hotta I, Imamura H, Takahashi K, Matsuura Y, Shirao T, Takai Y

Author

Akiko Mammoto MD, PhD Associate Professor in the Pediatrics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Binding Sites
Brain
Carrier Proteins
Contractile Proteins
Cytosol
Humans
In Vitro Techniques
Membrane Proteins
Microfilament Proteins
Molecular Sequence Data
Neuropeptides
Peptide Mapping
Profilins
Proline
Protein Binding
Rats
Recombinant Fusion Proteins