In:
Journal of Leukocyte Biology, Oxford University Press (OUP), Vol. 92, No. 2 ( 2012-08-01), p. 301-308
Abstract:
A new type of internalization domain highly conserved in IFNγ receptors across species, regulates human IFNγR1 endocytosis. This study tested the hypothesis that the IFN-γR1 287-YVSLI-91 intracellular motif regulates its endocytosis. IFN-γ exerts its biological activities by interacting with a specific cell-surface RC composed of two IFN-γR1 and two IFN-γR2 chains. Following IFN-γ binding and along with the initiation of signal transduction, the ligand and IFN-γR1 are internalized. Two major types of consensus-sorting signals are described in receptors, which are rapidly internalized from the plasma membrane to intracellular compartments: tyrosine-based and dileucine-based internalization motifs. Transfection of HEK 293 cells and IFN-γR1-deficient fibroblasts with WT and site-directed, mutagenesis-generated mutant IFN-γR1 expression vectors helped us to identify region IFN-γR1 287-YVSLI-291 as the critical domain required for IFN-γ-induced IFN-γR1 internalization and Y287 and LI290–291 as part of a common structure essential for receptor endocytosis and function. This new endocytosis motif, YxxLI, shares characteristics of tyrosine-based and dileucine-based internalization motifs and is highly conserved in IFN-γRs across species. The IFN-γR1 270-LI-271 dileucine motif, previously thought to be involved in this receptor endocytosis, showed to be unnecessary for receptor endocytosis.
Type of Medium:
Online Resource
ISSN:
1938-3673
,
0741-5400
Language:
English
Publisher:
Oxford University Press (OUP)
Publication Date:
2012
detail.hit.zdb_id:
2026833-6
SSG:
12
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