Interactions of drebrin and gephyrin with profilin.

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.

[1]  C. Field,et al.  Actin cytoskeleton: Are FH proteins local organizers? , 1997, Current Biology.

[2]  K. Nakao,et al.  p140mDia, a mammalian homolog of Drosophila diaphanous,is a target protein for Rho small GTPase and is a ligand for profilin , 1997, The EMBO journal.

[3]  T. Sasaki,et al.  Bni1p and Bnr1p: downstream targets of the Rho family small G‐proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae , 1997, The EMBO journal.

[4]  John R. Pringle,et al.  Bni1p, a Yeast Formin Linking Cdc42p and the Actin Cytoskeleton During Polarized Morphogenesis , 1997, Science.

[5]  T Watanabe,et al.  Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. , 1996, The EMBO journal.

[6]  C. Garner,et al.  Synaptic proteins and the assembly of synaptic junctions. , 1996, Trends in cell biology.

[7]  J. Wehland,et al.  Mena, a Relative of VASP and Drosophila Enabled, Is Implicated in the Control of Microfilament Dynamics , 1996, Cell.

[8]  A. Hall,et al.  Rho: a connection between membrane receptor signalling and the cytoskeleton. , 1996, Trends in cell biology.

[9]  M. Symons,et al.  Rho family GTPases: the cytoskeleton and beyond. , 1996, Trends in biochemical sciences.

[10]  S. Zigmond,et al.  Signal transduction and actin filament organization. , 1996, Current opinion in cell biology.

[11]  T. Sasaki,et al.  Rho as a regulator of the cytoskeleton. , 1995, Trends in biochemical sciences.

[12]  J. Kirsch,et al.  The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex , 1995, Current Opinion in Neurobiology.

[13]  U. Walter,et al.  The proline‐rich focal adhesion and microfilament protein VASP is a ligand for profilins. , 1995, The EMBO journal.

[14]  Wendell A. Lim,et al.  Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains , 1995, Nature.

[15]  T. Shirao The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review. , 1995, Journal of biochemistry.

[16]  T. Sasaki,et al.  Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells. , 1994, Biochemical and biophysical research communications.

[17]  R. H. Sohn,et al.  Profilin: At the crossroads of signal transduction and the actin cytoskeleton , 1994, BioEssays : news and reviews in molecular, cellular and developmental biology.

[18]  P Cicchetti,et al.  Identification of a ten-amino acid proline-rich SH3 binding site. , 1993, Science.

[19]  T. Sasaki,et al.  Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein. , 1992, The Journal of biological chemistry.

[20]  U. Walter,et al.  The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. , 1992, The EMBO journal.

[21]  G. Multhaup,et al.  Primary structure and alternative splice variants of gephyrin, a putative glycine receptor-tubulin linker protein , 1992, Neuron.

[22]  G. Bruns,et al.  Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis. , 1988, The Journal of biological chemistry.

[23]  Y. Matsuura,et al.  Baculovirus expression vectors: the requirements for high level expression of proteins, including glycoproteins. , 1987, The Journal of general virology.

[24]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[25]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[26]  A. Hall,et al.  Small GTP-binding proteins and the regulation of the actin cytoskeleton. , 1994, Annual review of cell biology.

[27]  K. Obata,et al.  Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. , 1992, Neuroreport.