Assembly of major histocompatibility complex class II subunits with invariant chain
نویسندگان
چکیده
منابع مشابه
The intracellular localization and oligomerization of chicken invariant chain with major histocompatibility complex class II subunits.
Invariant chain (Ii) binds to MHC class II (MHCII) to assemble a nonamer in the endoplasmic reticulum. Major histocompatibility complex class II-associated Ii peptide (CLIP) that occupies the peptide binding groove of MHCII prevents MHCII molecules from loading with endogenous antigens. We used the green or red fluorescent protein-fused Ii or MHCII subunits to detect the intracellular localizat...
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Peptides from the lumenal portion of invariant chain (Ii) spanning residues 80-106 (class II-associated Ii peptide [CLIP]) are found in association with several mouse and human major histocompatibility complex (MHC) class II allelic variants in wild-type and presentation-deficient mutant cells. The ready detection of these complexes suggests that such an intermediate is essential to the MHC cla...
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The binding of invariant chain to major histocompatibility complex (MHC) proteins is an important step in processing of MHC class II proteins and in antigen presentation. The question of how invariant chain can bind to all MHC class II proteins is central to understanding these processes. We have employed molecular modeling to predict the structure of class II-associated invariant chain peptide...
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During biosynthesis, MHC class II-invariant chain complexes are transported into endosomal compartments where invariant chain (Ii) is degraded and class II encounters antigenic peptides. One of the signals that determines this intracellular transport route has been localized to the cytosolic domain of Ii. Deletion of this signal disrupts endosomal targeting and results in the stable expression ...
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The intracellular transport and location of major histocompatibility complex (MHC) class II molecules and associated invariant chain (Ii) were investigated in a human melanoma cell line. In contrast to the class II molecules, which remain stable for greater than 4 h after synthesis, the associated Ii is proteolytically processed within 2 h. During or shortly after synthesis the NH2-terminal cyt...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2005
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2005.09.070