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不同的 SH3 结构域所表现出的独特泛素结合模式：分子决定因素及其功能意义。

Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.

机构信息

Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Granada, Spain ; Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

出版信息

PLoS One. 2013 Sep 11;8(9):e73018. doi: 10.1371/journal.pone.0073018. eCollection 2013.

DOI:10.1371/journal.pone.0073018
PMID:24039852
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3770644/
Abstract

SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination.

摘要

SH3 结构域构成了一种新型的泛素结合结构域。我们之前曾表明，CD2AP 的第三个 SH3 结构域 (SH3-C) 以另一种取向结合泛素。我们已经确定了第一个 CD2AP SH3 结构域和泛素之间复合物的结构，并进行了结构和突变分析，以破译 SH3-C 结合泛素的模式决定因素。我们发现，CD2AP 中的苯丙氨酸到酪氨酸突变以及同源的 CIN85 SH3-C 结构域中的突变并没有像之前的假设和我们对前两个 CD2AP SH3 结构域的发现那样，导致泛素结合的丧失。这些相关衔接蛋白的 SH3-C 结构域的类似替代结合模式的特点是对 C 端延伸的泛素分子具有更高的亲和力。我们得出结论，CD2AP/CIN85 SH3-C 结构域与泛素的相互作用构成了一种新的泛素结合模式，涉及到不同的细胞功能，从而改变了之前建立的 EGF 依赖性 CD2AP/CIN85 单泛素化机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/e7ed67f08619/pone.0073018.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/deaea3973964/pone.0073018.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/b3d91794da2d/pone.0073018.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/cd135eedf04e/pone.0073018.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/ce545bb456db/pone.0073018.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/08e59fcfe3df/pone.0073018.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/e7ed67f08619/pone.0073018.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/deaea3973964/pone.0073018.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/b3d91794da2d/pone.0073018.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/cd135eedf04e/pone.0073018.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/ce545bb456db/pone.0073018.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/08e59fcfe3df/pone.0073018.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cc81/3770644/e7ed67f08619/pone.0073018.g006.jpg

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