TRC40 can deliver short secretory proteins to the Sec61 translocon
| Autor: | Nicholas Johnson, Sven Lang, Richard Zimmermann, Stephen High, Pawel Leznicki, Fabio Vilardi |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
HSC70 Heat-Shock Proteins
Molecular Sequence Data Tail-anchored protein Biology Endoplasmic Reticulum 03 medical and health sciences Dogs 0302 clinical medicine Eeyarestatin I Asna 1 WRB protein Animals Humans Hydroxyurea Amino Acid Sequence Salivary Proteins and Peptides 030304 developmental biology 0303 health sciences Arsenite Transporting ATPases Endoplasmic reticulum 030302 biochemistry & molecular biology Hydrazones Membrane Proteins Membrane Transport Proteins Nuclear Proteins Intracellular Membranes Cell Biology Translocon SEC61 Translocon Transport protein Cell biology Protein Transport Secretory protein Post-translational translocation Membrane protein Apelin Intercellular Signaling Peptides and Proteins Rabbits Protein Processing Post-Translational SEC Translocation Channels 030217 neurology & neurosurgery Research Article |
| Zdroj: | Journal of Cell Science |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.102608 |
| Popis: | Summary Whilst the co-translational translocation of nascent proteins across the mammalian endoplasmic reticulum (ER) is well defined, the capacity of this organelle for post-translational translocation is poorly delineated. Here we identify two human secretory protein precursors, apelin and statherin, as bona fide substrates for post-translational translocation across the ER membrane. Further studies, in combination with Hyalophora cecropia preprocecropin A (ppcecA), show that all three proteins bind to TRC40 and can utilise this component for their delivery to the ER membrane in a well-established in vitro system. However, ppcecA is not an obligate TRC40 substrate, and it can also be delivered to the ER by an alternative TRC40-independent pathway. Upon arrival at the ER membrane, these short secretory proteins appear to be ubiquitously transported across the ER membrane through the Sec61 translocon, apparently irrespective of their delivery route. We speculate that the post-translational translocation of secretory proteins in higher eukaryotes is more prevalent than previously acknowledged. |
| Databáze: | OpenAIRE |
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