Abstract
Proper folding and assembly of major histocompatibility complex (MHC) class I complexes are essential for optimal peptide loading and subsequent antigen presentation. MHC class I folding involves the coordinated formation of multiple disulfide bonds within MHC class I molecules. However, the regulation of disulfide bond formation during the early process of MHC class I folding is uncharacterized. Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m). Depletion of PDI but not ERp57 by RNAi interfered with the disulfide bond formation in the MHC class I molecules. In the absence of PDI, the association of free class I heavy chain with calnexin increased, whereas the assembly of MHC class I heavy chain-beta(2)m heterodimers was delayed. These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m. Thus, our data establish a critical function for PDI in the early assembly of MHC class I molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 2553-2561 |
| Number of pages | 9 |
| Journal | Antioxidants & redox signaling |
| Volume | 11 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2009 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Physiology
- Molecular Biology
- Clinical Biochemistry
- Cell Biology
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A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules. / Kang, Kwonyoon; Park, Boyoun; Oh, Changhoon; Cho, Kwangmin; Ahn, Kwangseog.
In: Antioxidants & redox signaling, Vol. 11, No. 10, 01.01.2009, p. 2553-2561.Research output: Contribution to journal › Article
TY - JOUR
T1 - A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules.
AU - Kang, Kwonyoon
AU - Park, Boyoun
AU - Oh, Changhoon
AU - Cho, Kwangmin
AU - Ahn, Kwangseog
PY - 2009/1/1
Y1 - 2009/1/1
N2 - Proper folding and assembly of major histocompatibility complex (MHC) class I complexes are essential for optimal peptide loading and subsequent antigen presentation. MHC class I folding involves the coordinated formation of multiple disulfide bonds within MHC class I molecules. However, the regulation of disulfide bond formation during the early process of MHC class I folding is uncharacterized. Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m). Depletion of PDI but not ERp57 by RNAi interfered with the disulfide bond formation in the MHC class I molecules. In the absence of PDI, the association of free class I heavy chain with calnexin increased, whereas the assembly of MHC class I heavy chain-beta(2)m heterodimers was delayed. These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m. Thus, our data establish a critical function for PDI in the early assembly of MHC class I molecules.
AB - Proper folding and assembly of major histocompatibility complex (MHC) class I complexes are essential for optimal peptide loading and subsequent antigen presentation. MHC class I folding involves the coordinated formation of multiple disulfide bonds within MHC class I molecules. However, the regulation of disulfide bond formation during the early process of MHC class I folding is uncharacterized. Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m). Depletion of PDI but not ERp57 by RNAi interfered with the disulfide bond formation in the MHC class I molecules. In the absence of PDI, the association of free class I heavy chain with calnexin increased, whereas the assembly of MHC class I heavy chain-beta(2)m heterodimers was delayed. These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m. Thus, our data establish a critical function for PDI in the early assembly of MHC class I molecules.
UR - http://www.scopus.com/inward/record.url?scp=77952584245&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77952584245&partnerID=8YFLogxK
U2 - 10.1089/ars.2009.2465
DO - 10.1089/ars.2009.2465
M3 - Article
C2 - 19388826
AN - SCOPUS:77952584245
VL - 11
SP - 2553
EP - 2561
JO - Antioxidants and Redox Signaling
JF - Antioxidants and Redox Signaling
SN - 1523-0864
IS - 10
ER -