NMR Reveals the Interplay among the AMSH SH3 Binding Motif, STAM2, and Lys63-Linked Diubiquitin
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- 作者：Maggy Hologne1 ; Franç ; ois-Xavier Cantrelle2 ; Gwladys Riviere1 ; Florence Guilliè ; re1 ; Xavier Trivelli2 ; Olivier Walker1 ; olivier.walker@univ-lyon1.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：AMSH ; associated molecule with the SH3 domain of STAM ; AMSH-LP ; AMSH-like protein ; AMSH-SBM ; SBM motif of AMSH ; CHMP ; charged multivesicular body proteins ; CSP ; chemical shift perturbation ; ESCRT ; endosomal sorting complexes required for transport ; Hrs ; hepatocyte growth factor-regulated substrate ; HSQC ; heteronuclear single quantum coherence ; Lys63-Ub2 ; Lys63-linked diubiquitin ; Lys63-Ub3 ; Lys63-linked triubiquitin ; MD ; molecular dynamics ; 15N R2 ; 15N transverse spin relaxation rate ; NOE ; nucle
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：6 November 2016
- 年：2016
- 卷：428
- 期：22
- 页码：4544-4558
- 全文大小：1564 K
文摘
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The deubiquitinating enzyme AMSH specifically cleaves Lys63-linked polyubiquitin chains and increases its efficiency with the presence of the STAM protein.
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Both the UIM and the SH3 domain of the STAM2 protein interact with Lys63-Ub2.
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The SBM of AMSH outcompetes Lys63-Ub2 for SH3 binding.
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The SBM is unstructured in the free state and in complex with SH3.
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Overall, our findings and especially the AMSH-SBM/STAM2-SH3 structure reveal a possible structural organization and mechanism among AMSH, STAM, and Lys63-Ub2 chains.