Interaction of tapasin related protein with cell surface MHC class 1 heavy chain molecules.
نویسنده
چکیده
Tapasin related (TR) protein shares similarity (27%) with tapasin and is present in endoplasmic reticulam (ER) and on the cell surface of Hela cells. In the present article, TR protein was found localized in ER, but not in the lysosomes or late endosomes as studied by confocal colocalization. TR protein was associated with cell surface MHC class 1 HLA A2 heavy chain (HC) molecules and might be involved in chaperoning of cell surface HC MHC class 1 molecule. The results indicated that MHC class 1 cell surface molecules involved in antigen presentation of exogenous antigens, interact with cell surface chaperons.
منابع مشابه
Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alpha3 domain.
In human cells the association of MHC class I molecules with TAP is thought to be mediated by a third protein termed tapasin. We now show that tapasin is present in murine TAP-class I complexes as well. Furthermore, we demonstrate that a mutant H-2Dd molecule that does not interact with TAP due to a Glu to Lys mutation at residue 222 of the H chain (Dd(E222K)) also fails to bind to tapasin. Thi...
متن کاملThe role of tapasin in MHC class I protein trafficking in embryos and T cells.
Preimplantation mouse embryos express both classical (class Ia) and nonclassical (class Ib) MHC class I proteins, and yet are not rejected by the maternal immune system. Although the function of the embryonic MHC class Ia proteins is unknown, one MHC class Ib protein, Qa-2, the product of the preimplantation embryo development (Ped) gene, actually enhances reproductive success. Similar in struc...
متن کاملA charged amino acid residue in the transmembrane/cytoplasmic region of tapasin influences MHC class I assembly and maturation.
Tapasin influences the quantity and quality of MHC/peptide complexes at the cell surface; however, little is understood about the structural features that underlie its effects. Because tapasin, MHC class I, and TAP are transmembrane proteins, the tapasin transmembrane/cytoplasmic region has the potential to affect interactions at the endoplasmic reticulum membrane. In this study, we have assess...
متن کاملImmunodeficiency due to defective antigen processing: the molecular basis for type 1 bare lymphocyte syndrome.
(MHC) class I molecules are polymorphic cell surface glycoproteins that play an essential role in immune surveillance. In the MHC class I antigen presentation pathway, peptides derived from cytosolic proteasome-mediated proteolysis are transported into the endoplasmic reticulum (ER) via the transporter associated with antigen processing (TAP), reviewed in ref. 1. In the ER lumen, translocated p...
متن کاملTapasin is a facilitator, not an editor, of class I MHC peptide binding.
Tapasin has been proposed to function as a peptide editor to displace lower affinity peptides and/or to favor the binding of high affinity peptides. Consistent with this, cell surface HLA-B8 molecules in tapasin-deficient cells were less stable and the peptide repertoire was substantially altered. However, the binding affinities of peptides expressed in the absence of tapasin were unexpectedly ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Indian journal of experimental biology
دوره 47 10 شماره
صفحات -
تاریخ انتشار 2009