Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins
| Autor: | Christine M. Bentivoglio, Aaron D. Gitler, Charles Barlowe, Neil G. Margulis, Joshua D. Wilson, Nripesh Dhungel |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
biology Vesicle Endoplasmic reticulum Cell Biology COPI Golgi apparatus Biochemistry Cell biology 03 medical and health sciences Membrane glycoproteins symbols.namesake 030104 developmental biology Secretory protein Structural Biology Genetics biology.protein symbols Molecular Biology COPII Secretory pathway |
| Zdroj: | Traffic. 17:191-210 |
| ISSN: | 1398-9219 |
| DOI: | 10.1111/tra.12356 |
| Popis: | Coat protein complex II (COPII) vesicle formation at the endoplasmic reticulum (ER) transports nascent secretory proteins forward to the Golgi complex. To further define the machinery that packages secretory cargo and targets vesicles to Golgi membranes, we performed a comprehensive proteomic analysis of purified COPII vesicles. In addition to previously known proteins, we identified new vesicle proteins including Coy1, Sly41 and Ssp120, which were efficiently packaged into COPII vesicles for trafficking between the ER and Golgi compartments. Further characterization of the putative calcium-binding Ssp120 protein revealed a tight association with Emp47 and in emp47Δ cells Ssp120 was mislocalized and secreted. Genetic analyses demonstrated that EMP47 and SSP120 display identical synthetic positive interactions with IRE1 and synthetic negative interactions with genes involved in cell wall assembly. Our findings support a model in which the Emp47-Ssp120 complex functions in transport of plasma membrane glycoproteins through the early secretory pathway. |
| Databáze: | OpenAIRE |
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