Degradation of Newly Synthesized Polypeptides by Ribosome-Associated RACK1/c-Jun N-Terminal Kinase/Eukaryotic Elongation Factor 1A2 Complex
| Autor: | Gustavo J. Gutierrez, Shannon McLaughlan, Pedro Aza-Blanc, Tal Varsano, Yongmei Feng, Nahum Sonenberg, Valentina Gandin, Tiago Ferreira, Qingyan Au, Ivan Topisirovic, Tommy Alain, Ze'ev Ronai, Laurence M. Brill |
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| Rok vydání: | 2013 |
| Předmět: |
Proteasome Endopeptidase Complex
Molecular Sequence Data EEF1A2 MAP Kinase Kinase 7 Receptors Cell Surface Biology Receptors for Activated C Kinase Cell Line MAP2K7 Peptide Elongation Factor 1 Eukaryotic translation GTP-Binding Proteins Polysome Serine Animals Humans Eukaryotic Small Ribosomal Subunit Phosphorylation Molecular Biology Base Sequence Protein Stability JNK Mitogen-Activated Protein Kinases Translation (biology) Articles Cell Biology Neoplasm Proteins Cell biology Elongation factor Biochemistry Polyribosomes Peptides Ribosomes Signal Transduction |
| Zdroj: | Molecular and Cellular Biology. 33:2510-2526 |
| ISSN: | 1098-5549 |
| Popis: | Folding of newly synthesized polypeptides (NSPs) into functional proteins is a highly regulated process. Rigorous quality control ensures that NSPs attain their native fold during or shortly after completion of translation. Nonetheless, signaling pathways that govern the degradation of NSPs in mammals remain elusive. We demonstrate that the stress-induced c-Jun N-terminal kinase (JNK) is recruited to ribosomes by the receptor for activated protein C kinase 1 (RACK1). RACK1 is an integral component of the 40S ribosome and an adaptor for protein kinases. Ribosome-associated JNK phosphorylates the eukaryotic translation elongation factor 1A isoform 2 (eEF1A2) on serines 205 and 358 to promote degradation of NSPs by the proteasome. These findings establish a role for a RACK1/JNK/eEF1A2 complex in the quality control of NSPs in response to stress. |
| Databáze: | OpenAIRE |
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