Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51070Stonin homology domain (SHD) profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51070
Human stonins, like their Drosophila homologue stoned B are supposed to be endocytotic proteins involved in clathrin-mediated endocytosis at synapses. The two human stonins, as well as their Drosophila melanogaster and Caenorhabditis elegans homologues, exhibit a modular structure consisting of an N-terminal proline- and serine-rich domain, a central stonin homology domain (SHD), and a C-terminal domain homologous to the signal-binding domain of the mu subunits of adaptor protein (AP) complexes (mu-homology domain) (see <PDOC51072>). The ~140 amino-acid SHD domain has not been described in other proteins and may thus be unique to members of the stonin family. Its function is not yet known [1,2].
The profile we developed covers the entire SHD domain.
Last update:January 2005 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Martina J.A. Bonangelino C.J. Aguilar R.C. Bonifacino J.S. |
| Title | Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery. | |
| Source | J. Cell Biol. 153:1111-1120(2001). | |
| PubMed ID | 11381094 |
| 2 | Authors | Walther K. Diril M.K. Jung N. Haucke V. |
| Title | Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 101:964-969(2004). | |
| PubMed ID | 14726597 | |
| DOI | 10.1073/pnas.0307862100 |
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