A new member of the amphiphysin family connecting endocytosis and signal transduction pathways.

Src homology 3 (SH3) domains are conserved modules which participate in protein interaction by recognizing proline-rich motifs on target molecules. To identify new SH3-containing proteins, we performed a two-hybrid screen with a proline-rich region of human SOS-1. One of the specific SOS-1 interacting clones that were isolated from a mouse ...
brain cDNA library defines a new protein that was named amphiphysin 2 because of its homology to the previously reported amphiphysin. Amphiphysin 2 is expressed in a number of mouse tissues through multiple RNA transcripts. Here, we report the amino acid sequence of a brain form of amphiphysin 2 (BRAMP2) encoded by a 2. 5-kilobase mRNA. BRAMP2 associates in vitro with elements of the endocytosis machinery such as alpha-adaptin and dynamin. On a biosensor surface, the BRAMP2/dynamin interaction appeared to be direct and partly dependent on a proline-rich sequence of dynamin. Association with dynamin was also observed in PC12 cells after cell stimulation with nerve growth factor, suggesting that amphiphysin 2 may be connected to receptor-dependent signaling pathways. This hypothesis is strengthened by the ability of BRAMP2 to interact with the p21(ras) exchange factor SOS, in vitro, as a possible point of interconnection between the endocytic and signaling pathways.
Mesh Terms:
Adaptor Protein Complex alpha Subunits, Adaptor Proteins, Signal Transducing, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, DNA, Complementary, Dynamins, Endocytosis, Fungal Proteins, GTP Phosphohydrolases, Humans, Male, Membrane Proteins, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Nerve Tissue Proteins, PC12 Cells, Rats, Receptors, Cell Surface, Repressor Proteins, SOS1 Protein, Sequence Homology, Amino Acid, Signal Transduction, Tumor Suppressor Proteins
J. Biol. Chem.
Date: Jun. 13, 1997
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