HHV-7 U21 exploits Golgi quality control carriers to reroute class I MHC molecules to lysosomes
| Autor: | Melissa L. Whyte, Amy W. Hudson, Aaron T. Dirck |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Golgi Apparatus
Herpesvirus 7 Human Plasma protein binding Major histocompatibility complex Endoplasmic Reticulum Clathrin symbols.namesake Viral Proteins Humans Molecular Biology Integral membrane protein Golgi membrane biology Endoplasmic reticulum Histocompatibility Antigens Class I Cell Biology Articles Golgi apparatus Transport protein Cell biology Adaptor Proteins Vesicular Transport Protein Transport Membrane Trafficking symbols biology.protein Carrier Proteins Lysosomes HeLa Cells Protein Binding trans-Golgi Network |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 |
| Popis: | The human herpesvirus-7 (HHV-7) U21 glycoprotein binds to class I major histocompatibility complex (MHC) molecules in the endoplasmic reticulum (ER) and reroutes them to lysosomes. How this single viral glycoprotein efficiently redirects the U21/class I MHC complex to the lysosomal compartment is poorly understood. To investigate the trafficking of HHV-7 U21, we followed synchronous release of U21 from the ER as it traffics through the secretory system. Sorting of integral membrane proteins from the trans-Golgi network (TGN) has been shown to occur through tubular carriers that emanate from the TGN or through vesicular carriers that recruit GGA (Golgi-localized, γ-ear-containing, ARF-binding protein), clathrin adaptors, and clathrin. Here, we present evidence for the existence of a third type of Golgi-derived carrier that is vesicular, yet clathrin independent. This U21-containing carrier also carries a Golgi membrane protein engineered to form inducible oligomers. We propose that U21 employs the novel mechanism of forming oligomeric complexes with class I MHC molecules that result in sorting of the oligomeric U21/class I MHC complexes to Golgi--derived quality control carriers destined for lysosomes. |
| Databáze: | OpenAIRE |
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