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10.1038/srep44863 http://scihub22266oqcxt.onion/10.1038/srep44863 C5362955!5362955 !28332566     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28332566 &cmd=llinks): Failed to open stream: HTTP request failed! 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A conformational change within the WAVE2 complex regulates its degradation following cellular activation |pdf=|usr=}}{{28332566 }} gab.com Text A conformational change within the WAVE2 complex regulates its degradation following cellular activation JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28332566 #FOAvip WASp family Verprolin-homologous protein-2 (WAVE2), a member of the Wiskott-Aldrich syndrome protein (WASp) family of actin nucleation promoting factors, is a central regulator of actin cytoskeleton polymerization and dynamics. Multiple signaling pathways operate via WAVE2 to promote the actin-nucleating activity of the actin-related protein 2/3 (Arp2/3) complex. WAVE2 exists as a part of a pentameric protein complex known as the WAVE regulatory complex (WRC), which is unstable in the absence of its individual proteins. While the involvement of WAVE2 in actin polymerization has been well documented, its negative regulation mechanism is poorly characterized to date. Here, we demonstrate that WAVE2 undergoes ubiquitylation in a T-cell activation dependent manner, followed by proteasomal degradation. The WAVE2 ubiquitylation site was mapped to lysine 45, located at the N-terminus where WAVE2 binds to the WRC. Using Förster resonance energy transfer (FRET), we reveal that the autoinhibitory conformation of the WRC maintains the stability of WAVE2 in resting cells; the release of autoinhibition following T-cell activation facilitates the exposure of WAVE2 to ubiquitylation, leading to its degradation. The dynamic conformational structures of WAVE2 during cellular activation dictate its degradation. Twit Text FOAVip A conformational change within the WAVE2 complex regulates its degradation following cellular activation ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28332566 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28332566 #FOAvip English Wikipedia <ref>{{Cite pmid|28332566 }}</ref> A conformational change within the WAVE2 complex regulates its degradation following cellular activation #MMPMID28332566 Joseph N ; Biber G ; Fried S ; Reicher B ; Levy O ; Sabag B ; Noy E ; Barda-Saad M Sci Rep 2017[Mar]; 7 (ä): 44863 PMID28332566 show ga WASp family Verprolin-homologous protein-2 (WAVE2), a member of the Wiskott-Aldrich syndrome protein (WASp) family of actin nucleation promoting factors, is a central regulator of actin cytoskeleton polymerization and dynamics. Multiple signaling pathways operate via WAVE2 to promote the actin-nucleating activity of the actin-related protein 2/3 (Arp2/3) complex. WAVE2 exists as a part of a pentameric protein complex known as the WAVE regulatory complex (WRC), which is unstable in the absence of its individual proteins. While the involvement of WAVE2 in actin polymerization has been well documented, its negative regulation mechanism is poorly characterized to date. Here, we demonstrate that WAVE2 undergoes ubiquitylation in a T-cell activation dependent manner, followed by proteasomal degradation. The WAVE2 ubiquitylation site was mapped to lysine 45, located at the N-terminus where WAVE2 binds to the WRC. Using Förster resonance energy transfer (FRET), we reveal that the autoinhibitory conformation of the WRC maintains the stability of WAVE2 in resting cells; the release of autoinhibition following T-cell activation facilitates the exposure of WAVE2 to ubiquitylation, leading to its degradation. The dynamic conformational structures of WAVE2 during cellular activation dictate its degradation. |*Protein Conformation [MESH] |Amino Acids/metabolism [MESH] |Cell Line [MESH] |Humans [MESH] |Lymphocyte Activation/immunology [MESH] |Multiprotein Complexes/*chemistry/*metabolism [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Protein Interaction Domains and Motifs [MESH] |Protein Stability [MESH] |Proteolysis [MESH] |Receptors, Antigen, T-Cell/metabolism [MESH] |Structure-Activity Relationship [MESH] |T-Lymphocytes/immunology/metabolism [MESH] |Ubiquitination [MESH]A conformational change within the WAVE2 complex regulates its degrada(epmc).pdf DeepDyve Pubget Overpricing