HHV-7 U21 exploits Golgi quality control carriers to reroute class I MHC molecules to lysosomes. Mol Biol Cell 2020 Feb 01;31(3):196-208
Date
12/19/2019Pubmed ID
31851583Pubmed Central ID
PMC7001482DOI
10.1091/mbc.E19-07-0363Scopus ID
2-s2.0-85081146090 (requires institutional sign-in at Scopus site) 6 CitationsAbstract
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.
Author List
Dirck AT, Whyte ML, Hudson AWAuthor
Amy W. Hudson PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adaptor Proteins, Vesicular TransportCarrier Proteins
Clathrin
Endoplasmic Reticulum
Golgi Apparatus
HeLa Cells
Herpesvirus 7, Human
Histocompatibility Antigens Class I
Humans
Lysosomes
Protein Binding
Protein Transport
Viral Proteins
trans-Golgi Network
