The binding of syndapin SH3 domain to Dynamin proline-rich domain involves short and long distance elements. Luo, L., Xue, J., Kwan, A., Gamsjaeger, R., Wielens, J., Von Kleist, L., Cubeddu, L., Guo, Z., Stow, J., Parker, M., Mackay, J., & Robinson, P. Journal of Biological Chemistry, 291(18):9411-9424, 2016. doi abstract bibtex Dynamin is a GTPase that mediates vesicle fission during synaptic vesicle endocytosis. Its long C-terminal proline-rich domain contains 13 PXXP motifs, which orchestrate its interactions with multiple proteins. The SH3 domains of syndapin and endophilin bind the PXXP motifs called Site 2 and 3 (Pro-786-Pro-793) at the N-terminal end of the proline-rich domain, whereas the amphiphysin SH3 binds Site 9 (Pro-833-Pro-836) toward the C-terminal end. In some proteins, SH3/peptide interactions also involve short distance elements, which are 5-15 amino acid extensions flanking the central PXXP motif for high affinity binding. Here we found two previously unrecognized elements in the central and the C-terminal end of the dynamin proline-rich domain that account for a significant increase in syndapin binding affinity compared with a previously reported Site 2 and Site 3 PXXP peptide alone. The first new element (Gly-807-Gly-811) is short distance element on the C-terminal side of Site 2 PXXP, which might contact a groove identified under the RT loop of the SH3 domain. The second element (Arg-838-Pro-844) is located about 50 amino acids downstream of Site 2. These two elements provide additional specificity tothe syndapin SH3 domain outsideofthe well described polyproline-binding groove. Thus, the dynamin/syndapin interaction is mediated via a network of multiple contacts outside the core PXXP motif over a previously unrecognized extended region of the proline-rich domain. To our knowledge this is the first example among known SH3 interactions to involve spatially separated and extended long-range elements that combine to provide a higher affinity interaction. 7copy;2016 by The American Society for Biochemistry and Molecular Biology, Inc.
@article{
title = {The binding of syndapin SH3 domain to Dynamin proline-rich domain involves short and long distance elements},
type = {article},
year = {2016},
pages = {9411-9424},
volume = {291},
id = {34917dfc-3a3c-379e-a481-47c891a62429},
created = {2023-01-10T01:44:29.922Z},
file_attached = {false},
profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
last_modified = {2023-01-10T01:44:29.922Z},
read = {false},
starred = {false},
authored = {false},
confirmed = {false},
hidden = {false},
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abstract = {Dynamin is a GTPase that mediates vesicle fission during synaptic vesicle endocytosis. Its long C-terminal proline-rich domain contains 13 PXXP motifs, which orchestrate its interactions with multiple proteins. The SH3 domains of syndapin and endophilin bind the PXXP motifs called Site 2 and 3 (Pro-786-Pro-793) at the N-terminal end of the proline-rich domain, whereas the amphiphysin SH3 binds Site 9 (Pro-833-Pro-836) toward the C-terminal end. In some proteins, SH3/peptide interactions also involve short distance elements, which are 5-15 amino acid extensions flanking the central PXXP motif for high affinity binding. Here we found two previously unrecognized elements in the central and the C-terminal end of the dynamin proline-rich domain that account for a significant increase in syndapin binding affinity compared with a previously reported Site 2 and Site 3 PXXP peptide alone. The first new element (Gly-807-Gly-811) is short distance element on the C-terminal side of Site 2 PXXP, which might contact a groove identified under the RT loop of the SH3 domain. The second element (Arg-838-Pro-844) is located about 50 amino acids downstream of Site 2. These two elements provide additional specificity tothe syndapin SH3 domain outsideofthe well described polyproline-binding groove. Thus, the dynamin/syndapin interaction is mediated via a network of multiple contacts outside the core PXXP motif over a previously unrecognized extended region of the proline-rich domain. To our knowledge this is the first example among known SH3 interactions to involve spatially separated and extended long-range elements that combine to provide a higher affinity interaction. 7copy;2016 by The American Society for Biochemistry and Molecular Biology, Inc.},
bibtype = {article},
author = {Luo, L. and Xue, J. and Kwan, A. and Gamsjaeger, R. and Wielens, J. and Von Kleist, L. and Cubeddu, L. and Guo, Z. and Stow, J.L. and Parker, M.W. and Mackay, J.P. and Robinson, P.J.},
doi = {10.1074/jbc.M115.703108},
journal = {Journal of Biological Chemistry},
number = {18}
}
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Its long C-terminal proline-rich domain contains 13 PXXP motifs, which orchestrate its interactions with multiple proteins. The SH3 domains of syndapin and endophilin bind the PXXP motifs called Site 2 and 3 (Pro-786-Pro-793) at the N-terminal end of the proline-rich domain, whereas the amphiphysin SH3 binds Site 9 (Pro-833-Pro-836) toward the C-terminal end. In some proteins, SH3/peptide interactions also involve short distance elements, which are 5-15 amino acid extensions flanking the central PXXP motif for high affinity binding. Here we found two previously unrecognized elements in the central and the C-terminal end of the dynamin proline-rich domain that account for a significant increase in syndapin binding affinity compared with a previously reported Site 2 and Site 3 PXXP peptide alone. The first new element (Gly-807-Gly-811) is short distance element on the C-terminal side of Site 2 PXXP, which might contact a groove identified under the RT loop of the SH3 domain. The second element (Arg-838-Pro-844) is located about 50 amino acids downstream of Site 2. These two elements provide additional specificity tothe syndapin SH3 domain outsideofthe well described polyproline-binding groove. Thus, the dynamin/syndapin interaction is mediated via a network of multiple contacts outside the core PXXP motif over a previously unrecognized extended region of the proline-rich domain. To our knowledge this is the first example among known SH3 interactions to involve spatially separated and extended long-range elements that combine to provide a higher affinity interaction. 7copy;2016 by The American Society for Biochemistry and Molecular Biology, Inc.","bibtype":"article","author":"Luo, L. and Xue, J. and Kwan, A. and Gamsjaeger, R. and Wielens, J. and Von Kleist, L. and Cubeddu, L. and Guo, Z. and Stow, J.L. and Parker, M.W. and Mackay, J.P. and Robinson, P.J.","doi":"10.1074/jbc.M115.703108","journal":"Journal of Biological Chemistry","number":"18","bibtex":"@article{\n title = {The binding of syndapin SH3 domain to Dynamin proline-rich domain involves short and long distance elements},\n type = {article},\n year = {2016},\n pages = {9411-9424},\n volume = {291},\n id = {34917dfc-3a3c-379e-a481-47c891a62429},\n created = {2023-01-10T01:44:29.922Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:44:29.922Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {Dynamin is a GTPase that mediates vesicle fission during synaptic vesicle endocytosis. 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The second element (Arg-838-Pro-844) is located about 50 amino acids downstream of Site 2. These two elements provide additional specificity tothe syndapin SH3 domain outsideofthe well described polyproline-binding groove. Thus, the dynamin/syndapin interaction is mediated via a network of multiple contacts outside the core PXXP motif over a previously unrecognized extended region of the proline-rich domain. 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