Association of Major Histocompatibility Complex II with Cholesterol- and Sphingolipid-rich Membranes Precedes Peptide Loading

Karacsonyi, Claudia; Knorr, Ruth; Fülbier, Angela; Lindner, Robert

doi:10.1074/jbc.m404608200

Cited by 16 publications

(46 citation statements)

References 66 publications

(83 reference statements)

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“…AP, alkaline phosphatase; con, control; MCD, β-methyl-cyclodextrin. been reported, but MHC I has not been found to co-cluster with this molecule (Anderson et al, 2000;Goebel et al, 2002;Huby et al, 1999;Karacsonyi et al, 2004). We confirmed these data and also demonstrated that there was only limited co-patching of MHC I and MHC II, suggesting that these proteins prefer distinct membrane environments.…”

Section: The Membrane Environment Of Mhc Proteinssupporting

confidence: 79%

“…Thus, the rigorous extraction procedure separated DRMs containing MHC I or MHC II. In agreement with earlier results, CD81, a marker for tetraspanin domains at the plasma membrane, was largely solubilized (Karacsonyi et al, 2004). Only residual amounts of this protein were detected in a position close to MHC II-containing DRMs.…”

Section: Distribution Of Mhc Proteins To Distinct Drmssupporting

confidence: 79%

“…Only residual amounts of this protein were detected in a position close to MHC II-containing DRMs. The maturely glycosylated form of MHC II-associated invariant chain was detected in gradient fractions slightly denser than light DRMs (data not shown), as described earlier (Karacsonyi et al, 2004). Some ICAM1 floated in light DRMs but not in dense ones (Fig.…”

Section: Distribution Of Mhc Proteins To Distinct Drmssupporting

confidence: 63%

“…There is biophysical evidence for membrane raft association of MHC I (Bodnar et al, 2003;Matko et al, 1994); however, neither DRM association nor co-patching with G M 1 have been detected (Goebel et al, 2002;Karacsonyi et al, 2004;Naslavsky et al, 2004), except for one report on indirect raft association via ICAM1 (Lebedeva et al, 2004). Although these data suggest that MHC I and MHC II differ in their membrane raft association, a colocalization of MHC I and MHC II in 'supermolecular receptor clusters' has also been reported (Jenei et al, 1997;Vamosi et al, 2004).…”

Section: Introductionmentioning

confidence: 63%

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Endocytosis of MHC molecules by distinct membrane rafts

Knorr

Karacsonyi

Lindner

2009

Journal of Cell Science

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In B-lymphocytes, endocytosis of MHC I and MHC II molecules is important for the cross-priming and presentation of labile antigens, respectively. Here, we report that MHC I and MHC II were internalized by separate endocytic carriers that lacked transferrin receptor. Cholera toxin B was co-internalized with MHC II, but not with MHC I, suggesting that the CLIC/GEEC pathway is involved in the uptake of MHC II. Endocytosis of MHC I and MHC II was inhibited by filipin, but only MHC II showed a strong preference for a membrane raft environment in a co-clustering analysis with GM1. By using a novel method for the extraction of detergent-resistant membranes (DRMs), we observed that MHC I and MHC II associate with two distinct types of DRMs. These differ in density, protein content, lipid composition, and ultrastructure. The results of cell surface biotinylation and subsequent DRM isolation show that precursors for both DRMs coexist in the plasma membrane. Moreover, clustering of MHC proteins at the cell surface resulted in shifts of the respective DRMs, revealing proximity-induced changes in the membrane environment. Our results suggest that the preference of MHC I and MHC II for distinct membrane rafts directs them to different cellular entry points.

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Section: The Membrane Environment Of Mhc Proteinssupporting

confidence: 79%

Section: Distribution Of Mhc Proteins To Distinct Drmssupporting

confidence: 79%

Section: Distribution Of Mhc Proteins To Distinct Drmssupporting

confidence: 63%

Section: Introductionmentioning

confidence: 63%

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Endocytosis of MHC molecules by distinct membrane rafts

Knorr

Karacsonyi

Lindner

2009

Journal of Cell Science

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“…In contrast to MHCII -Ii complexes, pMHCII is endocytosed via clathrin-and dynamin-independent pathway(s), possibly involving SWAP-70-regulated RhoA/ RhoB (Ocana-Morgner et al 2009) or Arf6-and Rab35-dependent mechanism(s) (Walseng et al 2008). MHCII is found in detergent-resistant membrane domains (DRMs) (Anderson et al 2000;Karacsonyi et al 2004;Rodgers and Smith 2005), and endocytosis of MHCII was severely hampered after treatment of cells with Filipin, a cholesterol-sequestering agent (Knorr et al 2009). Perhaps pMHCII uses the clathrinindependent carrier (GLIC)/GPI-AP-enriched early endosomal compartment (GEEC) pathway, an endocytosis route that is also used by lipid raft-associated molecules like GPI-linked proteins and cholera toxin B (Mayor and Pagano 2007;Howes et al 2010).…”

Section: Trafficking Of Pmhciimentioning

confidence: 99%

MHC Class II Antigen Presentation by Dendritic Cells Regulated through Endosomal Sorting

Broeke

Wubbolts

Stoorvogel

2013

Cold Spring Harbor Perspectives in Biology

142

102

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For the initiation of adaptive immune responses, dendritic cells present antigenic peptides in association with major histocompatibility complex class II (MHCII) to naïve CD4 þ T lymphocytes. In this review, we discuss how antigen presentation is regulated through intracellular processing and trafficking of MHCII. Newly synthesized MHCII is chaperoned by the invariant chain to endosomes, where peptides from endocytosed pathogens can bind. In nonactivated dendritic cells, peptide-loaded MHCII is ubiquitinated and consequently sorted by the ESCRT machinery to intraluminal vesicles of multivesicular bodies, ultimately leading to lysosomal degradation. Ubiquitination of newly synthesized MHCII is blocked when dendritic cells are activated, now allowing its transfer to the cell surface. This mode of regulation for MHCII is a prime example of how molecular processing and sorting at multivesicular bodies can determine the expression of signaling receptors at the plasma membrane.

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Ligand Selection and Trafficking for MHC II

Mellins

2016

Encyclopedia of Immunobiology

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Association of Major Histocompatibility Complex II with Cholesterol- and Sphingolipid-rich Membranes Precedes Peptide Loading

Cited by 16 publications

References 66 publications

Endocytosis of MHC molecules by distinct membrane rafts

Endocytosis of MHC molecules by distinct membrane rafts

MHC Class II Antigen Presentation by Dendritic Cells Regulated through Endosomal Sorting

Ligand Selection and Trafficking for MHC II

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