The SH3 Domains of Endophilin and Amphiphysin Bind to the Proline-rich Region of Synaptojanin 1 at Distinct Sites That Display an Unconventional Binding Specificity-Reference-Cited by-同舟云学术

The SH3 Domains of Endophilin and Amphiphysin Bind to the Proline-rich Region of Synaptojanin 1 at Distinct Sites That Display an Unconventional Binding Specificity

Published:1999-11 Issue:45 Volume:274 Page:32001-32007
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cestra Gianluca,Castagnoli Luisa,Dente Luciana,Minenkova Olga,Petrelli Annalisa,Migone Nicola,Hoffmüller Ulrich,Schneider-Mergener Jens,Cesareni Gianni

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. The GTPase dynamin binds to and is activated by a subset of SH3 domains

2. Interaction of Grb2 via its Src homology 3 domains with synaptic proteins including synapsin I.

3. Identification of the Major Synaptojanin-binding Proteins in Brain

4. The Src Homology Domain 3 (SH3) of a Yeast Type I Myosin, Myo5p, Binds to Verprolin and Is Required for Targeting to Sites of Actin Polarization

5. Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity

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