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Interactions of drebrin and gephyrin with profilin.

Authors: Mammoto, A  Sasaki, T  Asakura, T  Hotta, I  Imamura, H  Takahashi, K  Matsuura, Y  Shirao, T  Takai, Y 
Citation: Mammoto A, etal., Biochem Biophys Res Commun. 1998 Feb 4;243(1):86-9.
Pubmed: (View Article at PubMed) PMID:9473484
DOI: Full-text: DOI:10.1006/bbrc.1997.8068

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.


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CRRD Object Information
CRRD ID: 8553893
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.