NDLI: An endocytic YXXΦ (YRRF) cargo sorting motif in the cytoplasmic tail of murine cytomegalovirus AP2 ‘adapter adapter’ protein m04/gp34 antagonizes virus evasion of natural killer cells

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An endocytic YXXΦ (YRRF) cargo sorting motif in the cytoplasmic tail of murine cytomegalovirus AP2 ‘adapter adapter’ protein m04/gp34 antagonizes virus evasion of natural killer cells

Content Provider	Springer Nature Link
Author	Fink, Annette Blaum, Franziska Babic Cac, Marina Ebert, Stefan Lemmermann, Niels A. W. Reddehase, Matthias J.
Copyright Year	2015
Abstract	Viruses have evolved proteins that bind immunologically relevant cargo molecules at the cell surface for their downmodulation by internalization. Via a tyrosine-based sorting motif YXXΦ in their cytoplasmic tails, they link the bound cargo to the cellular adapter protein-2 (AP2), thereby sorting it into clathrin-triskelion-coated pits for accelerated endocytosis. Downmodulation of CD4 molecules by lentiviral protein NEF represents the most prominent example. Based on connecting cargo to cellular adapter molecules, such specialized viral proteins have been referred to as ‘connectors’ or ‘adapter adapters.’ Murine cytomegalovirus glycoprotein m04/gp34 binds stably to MHC class-I (MHC-I) molecules and suspiciously carries a canonical YXXΦ endocytosis motif YRRF in its cytoplasmic tail. Disconnection from AP2 by motif mutation ARRF should retain m04-MHC-I complexes at the cell surface and result in an enhanced silencing of natural killer (NK) cells, which recognize them via inhibitory receptors. We have tested this prediction with a recombinant virus in which the AP2 motif is selectively destroyed by point mutation Y248A, and compared this with the deletion of the complete protein in a Δm04 mutant. Phenotypes were antithetical in that loss of AP2-binding enhanced NK cell silencing, whereas absence of m04-MHC-I released them from silencing. We thus conclude that AP2-binding antagonizes NK cell silencing by enhancing endocytosis of the inhibitory ligand m04-MHC-I. Based on a screen for tyrosine-based endocytic motifs in cytoplasmic tail sequences, we propose here the new hypothesis that most proteins of the m02–m16 gene family serve as ‘adapter adapters,’ each selecting its specific cell surface cargo for clathrin-assisted internalization.
Starting Page	383
Ending Page	394
Page Count	12
File Format	PDF
ISSN	03008584
Journal	Medical Microbiology and Immunology
Volume Number	204
Issue Number	3
e-ISSN	14321831
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2015-04-08
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Adapter protein (AP2) Cargo sorting Clathrin-mediated endocytosis Endocytosis motif Immune evasion Tyrosine-based motif YXXΦ Medical Microbiology Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology Microbiology (medical)

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An endocytic YXXΦ (YRRF) cargo sorting motif in the cytoplasmic tail of murine cytomegalovirus AP2 ‘adapter adapter’ protein m04/gp34 antagonizes virus evasion of natural killer cells

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