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10.1038/ncomms15730 http://scihub22266oqcxt.onion/10.1038/ncomms15730 C5467238!5467238 !28589942     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28589942 &cmd=llinks): Failed to open stream: HTTP request failed! 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Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex |pdf=|usr=}}{{28589942 }} gab.com Text Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28589942 #FOAvip Misfolded polypeptides are rapidly cleared from cells via the ubiquitin-proteasome system (UPS). However, when the UPS is impaired, misfolded polypeptides form small cytoplasmic aggregates, which are sequestered into an aggresome and ultimately degraded by aggrephagy. Despite the relevance of the aggresome to neurodegenerative proteinopathies, the molecular mechanisms underlying aggresome formation remain unclear. Here we show that the CTIF-eEF1A1-DCTN1 (CED) complex functions in the surveillance of either pre-existing or newly synthesized polypeptides by linking two molecular events: selective recognition and aggresomal targeting of misfolded polypeptides. These events are accompanied by CTIF sequestration into the aggresome, preventing the additional synthesis of misfolded polypeptides from mRNAs bound by nuclear cap-binding complex. These events render cells more resistant to apoptosis induced by proteotoxic stresses. Collectively, our data provide compelling evidence for a previously unappreciated protein surveillance pathway and a regulatory gene expression network for coping with misfolded polypeptides. Twit Text FOAVip Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28589942 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28589942 #FOAvip English Wikipedia <ref>{{Cite pmid|28589942 }}</ref> Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex #MMPMID28589942 Park J ; Park Y ; Ryu I ; Choi MH ; Lee HJ ; Oh N ; Kim K ; Kim KM ; Choe J ; Lee C ; Baik JH ; Kim YK Nat Commun 2017[Jun]; 8 (ä): 15730 PMID28589942 show ga Misfolded polypeptides are rapidly cleared from cells via the ubiquitin-proteasome system (UPS). However, when the UPS is impaired, misfolded polypeptides form small cytoplasmic aggregates, which are sequestered into an aggresome and ultimately degraded by aggrephagy. Despite the relevance of the aggresome to neurodegenerative proteinopathies, the molecular mechanisms underlying aggresome formation remain unclear. Here we show that the CTIF-eEF1A1-DCTN1 (CED) complex functions in the surveillance of either pre-existing or newly synthesized polypeptides by linking two molecular events: selective recognition and aggresomal targeting of misfolded polypeptides. These events are accompanied by CTIF sequestration into the aggresome, preventing the additional synthesis of misfolded polypeptides from mRNAs bound by nuclear cap-binding complex. These events render cells more resistant to apoptosis induced by proteotoxic stresses. Collectively, our data provide compelling evidence for a previously unappreciated protein surveillance pathway and a regulatory gene expression network for coping with misfolded polypeptides. |*Apoptosis [MESH] |*Protein Folding [MESH] |Autophagy [MESH] |Biological Transport [MESH] |Cytoplasm/chemistry [MESH] |Down-Regulation [MESH] |HEK293 Cells [MESH] |HeLa Cells [MESH] |Humans [MESH] |Inclusion Bodies/*chemistry [MESH] |Peptide Elongation Factor 1/*chemistry [MESH] |Peptides/*chemistry [MESH] |Proteasome Endopeptidase Complex/*chemistry [MESH] |Protein Binding [MESH] |Protein Denaturation [MESH] |Protein Transport [MESH]Misfolded polypeptides are selectively recognized and transported towa(epmc).pdf DeepDyve Pubget Overpricing