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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Ringstad, N. Nemoto, Y. De Camilli, P. |
Description | Author Affiliation: Ringstad N ( Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.); |
Abstract | The GTPase dynamin I and the inositol 5-phosphatase synaptojanin are nerve terminal proteins implicated in synaptic vesicle recycling. Both proteins contain COOH-terminal proline-rich domains that can interact with a variety of Src homology 3 (SH3) domains. A major physiological binding partner for dynamin I and synaptojanin in the nervous system is amphiphysin I, an SH3 domain-containing protein also concentrated in nerve terminals. We have used the proline-rich tail of synaptojanin to screen a rat brain library by the two-hybrid method to identify additional interacting partners of synaptojanin. Three related proteins containing SH3 domains that are closely related to the SH3 domains of Grb2 were isolated: SH3p4, SH3p8, and SH3p13. Further biochemical studies demonstrated that the SH3p4/8/13 proteins bind to both synaptojanin and dynamin I. The SH3p4/8/13 transcripts are differentially expressed in tissues: SH3p4 mRNA was detected only in brain, SH3p13 mRNA was present in brain and testis, and the SH3p8 transcript was detected at similar levels in multiple tissues. Members of the SH3p4/8/13 protein family were found to be concentrated in nerve terminals, and pools of synaptojanin and dynamin I were coprecipitated from brain extracts with antibodies recognizing SH3p4/8/13. These findings underscore the important role of SH3-mediated interactions in synaptic vesicle recycling. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 16 |
Volume Number | 94 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 1997-09-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Adaptor Proteins, Signal Transducing Brain Metabolism Carrier Proteins Nerve Tissue Proteins Phosphoric Monoester Hydrolases Proteins Receptor, Epidermal Growth Factor Chemistry Src Homology Domains Amino Acid Sequence Animals Binding Sites Genetics Molecular Sequence Data Organ Specificity Saccharomyces Cerevisiae Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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