Der MHC-Klasse-II-Komplex besteht aus zwei etwa gleich großen membranverankerten Proteinuntereinheiten, einer α- und einer β-Untereinheit, die jeweils weiter in zwei Domänen (α1 und α2, β1 und β2) unterteilt werden können. Im Gegensatz zum MHC-Klasse-I-Komplex sind beim MHC-Klasse-II-Komplex beide Untereinheiten in der Zellmembran verankert Dieses wird CLIP (class-II-associated invariant chain peptide) genannt und verhindert weiterhin die Bindung eines Peptids. Um ein Peptid aus dem Endosom binden zu können muss der CLIP dissoziieren oder abgespalten werden. Dieser Vorgang wird durch ein weiteres MHC-Klasse-II-Komplex katalysiert, beim Menschen HLA-DM genannt Without the invariant chain, the alpha and beta proteins will not associate. Invariant chain (Ii) which trimerizes in the ER, associates with MHC class II molecules and is released from the ER as a nine subunit complex. This MHC-invariant complex passes from the RER to, and out of, the Golgi body. Before moving to the cell surface, the vesicle containing this complex fuses with an endocytic compartment where an external protein has been broken into fragments. Here the invariant chain is. MHC II wird nur von bestimmten Zellen, z. B. von dendritischen Zellen, exprimiert. Die Peptid-Bindungstasche dieses Komplexes wird - solange er sich im ER befindet - durch eine invariant chain, ebenfalls ein Peptid, blockiert The invariant chain (Ii) is a transmembrane protein that associates with the MHC class II molecules in the endoplasmic reticulum. Expression of II in MHC class II-negative CV1 cells showed that it acquired complex-type oligosaccharide side chains and was retained in endosomal compartments. To search for a sorting signal, we made progressive deletions from the cytoplasmic N-terminus of Ii
Ii, invariant chain; MHC II, major histocompatibility complex class II molecule(s); MVB, multivesicular bodies; MIIC, MHC class II rich compartment; M6PR, mannose 6-phosphate recep-tor; TGN, trans-Golgi network; TfR, transferrin receptor * Corresponding author. Fax: +33-1-42-34-64-38. E-mail address: email@example.com (P. Benaroch). BBAMCR 14817 5-2-02 Biochimica et Biophysica Acta 1542 (2002. . Pre-clinical studies evaluating the fusion of Ii to antigens encoded in vector delivery systems have shown that this strategy may enhance T cell immune responses to the encoded antigen. We now assess this strategy in.
The conserved invariant chain associates with highly polymorphic alpha and beta subunits guiding class II transport through the secretory pathway. Early associations of these three polypeptides inside antigen-presenting cells are poorly understood. The present experiments provide a detailed picture Allelic differences affecting invariant chain dependency of MHC class II subunit assembly. MHC II assembly in the ER and trafficking to endosomes is guided by a specialized MHC II chaperone termed the invariant chain (Ii). Ii self‐associates into a trimer in the ER, this provides a scaffold for the assembly of three MHC II heterodimers and blocks their peptide binding grooves, thereby avoiding premature peptide binding. Ii then transports the nascent MHC II to more or less. Serves as cell surface receptor for the cytokine MIF. Class-II-associated invariant chain peptide: Binds to the peptide-binding site of MHC class II alpha/beta heterodimers forming an alpha-beta-CLIP complex, thereby preventing the loading of antigenic peptides to the MHC class II complex until its release by HLA-DM in the endosome.1 Publicatio . 2. The abbreviations used are: Ii . invariant chain. APC. antigen-presenting cell. ER. endoplasmic reticulum. The Ii is degraded until only a small fragment, dubbed CLIP, remains bound in the peptide-binding groove. Lysosomal pH and the class II-like.
HLA class II histocompatibility antigen gamma chain also known as HLA-DR antigens-associated invariant chain or CD74, is a protein that in humans is encoded by the CD74 gene. The invariant chain is a polypeptide which plays a critical role in antigen presentation. It is involved in the formation and transport of MHC class II peptide complexes for the generation of CD4+ T cell responses. The cell surface form of the invariant chain is known as CD74. CD74 is a cell surface receptor for the cytoki . The Invariant chain contains a single transmembrane domain. Ii first assembles into a trimer and then associates with three class II alpha/beta MHC heterodimers The invariant chain (Ii; CD74) has multiple functions but is best characterized as the main MHC class II (MHCII) chaperone. Ii is a type II protein consisting of a short cytoplasmic tail, a transmembrane region and a luminal domain that can be further partitioned into a membrane-proximal disordered region, the main MHCII-interacting sequence (CLIP), and a C-terminal trimerization domain (1, 2) The MHC class II invariant chain (Ii or CD74) in higher vertebrates is necessary for normal MHC class II loading in endosomal compartments. Detection of an Ii chain in fish would greatly support the idea that MHC class II function in fish and higher vertebrates is similar. Before this study only Ii homologues had been reported in fish that are unlikely to perform true Ii function
MHC II and the Endocytic Pathway: Regulation by Invariant Chain Structure of MHC II and Ii. Whereas MHC class I (MHC I) is ubiquitously expressed on all nucleated cells, the expression... Expression and regulation of MHC II/Ii. In the APC lineages MHC II gene expression is modulated as a function of. Pieters J, Bakke O, Dobberstein B: The MHC class II-associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail. J Cell Sci 1993;106:831-846. PubMed; CAS; Google Scholar; 43. Letourneur F, Klausner R: A novel di-leucine motif and a tyrosinebased motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 1992;69:1143-1157. PubMed. UniProtKB. x; UniProtKB. Protein knowledgebase. UniParc. Sequence archive. Help. Help pages, FAQs, UniProtKB manual, documents, news archive and Biocuration projects Intracellular transport of class II MHC molecules directed by invariant chain. Vincent Lotteau 1, Luc Teyton 1, Annick Peleraux 1, Tommy Nilsson 1 nAff2, Lars Karlsson 1, Sandra L. Schmid 1, Vito.
Ii, invariant chain; MHC II, major histocompatibility complex class II molecule(s); MVB, multivesicular bodies; MIIC, MHC class II rich compartment; M6PR, mannose 6-phosphate recep-tor; TGN, trans-Golgi network; TfR, transferrin receptor * Corresponding author. Fax: +33-1-42-34-64-38. E-mail address: firstname.lastname@example.org (P. Benaroch). BBAMCR 14817 5-2-02 Biochimica et Biophysica Acta 1542 (2002. Coalescence of B cell receptor and invariant chain MHC II in a raft‐like membrane domain. Julian T. Hauser. Hannover Medical School, Department of Cell Biology, Center for Anatomy, Hannover, Germany. Search for more papers by this author . Robert Lindner. Corresponding Author. E-mail address: lindner.robert@mh‐hannover.de. Hannover Medical School, Department of Cell Biology, Center for. Interaction of invariant chain trimer and MHC II alpha beta dimer Stable Identifier. R-HSA-2130478. Type.
Class II associated invariant chain peptide) gebildet werden, die die MHC-Grube blockieren. Danach erfolgt der Austausch der CLIPs gegen richtige Peptide, die von speziellen, im sauren pH aktiven lysosomalen Proteasen produziert werden. Die fertig beladenen MHC-II-Moleküle werden dann an die Zelloberfläche gebracht. Von den in der Peptidbindungsgrube fixierten neun Aminosäuren eines MHC. Major histocompatibility complex (MHC) class II-associated invariant chain (Ii) plays a critical role in antigen presentation, forming MHC class II peptide complexes for the generation of CD4+ T cell responses. Preclinical studies evaluating the fusion of Ii to antigens encoded in vector delivery systems have shown that this strategy may enhance T cell immune responses to the encoded antigen.
The transmembrane (TM) domain of the major histocompatibility complex (MHC) class II-associated invariant chain (Ii) has long been implicated in both correct folding and function of the MHC class II complex. To function correctly, Ii must form a trimer, and the TM domain is one of the domains thought to stabilize the trimeric state. Specific mutations in the TM domain have been shown. The invariant chain (Ii; CD74) plays a critical role in this process by influencing the expression and peptide loading of the MHC class II molecules. Therefore, coordinate expression of these molecules is believed to play an important role in antigen presentation. This study explores the expression of these molecules in fetal tissues. Formalin-fixed, paraffin-embedded multi-organ tissue blocks. Rho GTPase Cdc42 controls invariant chain processing and MHC II loading in Dendritic Cells von mir selbständig und ohne unerlaubte Hilfe angefertigt wurde. Ich habe mich dabei keiner anderen als der von mir ausdrücklich bezeichneten Hilfen und Quellen bedient. Die Dissertation wurde in der jetzigen oder ähnlichen Form bei keiner anderen Hochschule eingereicht und hat auch noch keinen.
MHC class II molecules consist of an also been associated with juvenile dermatomyositis (12).and chain and are transported to endosomal-lysosomal compartments by the invariant chain (Ii).2 The Ii is degraded until only a small fragment, dubbed CLIP, remains bound in the peptide-binding groove. Lysosomal pH and the class II-like molecule HLA-DM promote the exchange of the CLIP fragment for more. Invariant chain (Ii) formt einen Komplex mit MHC II, blockiert die Bindung von Peptiden und miss-gefalteten Proteinen. Ii wird in einem sauren Endosom gespalten, lässt kurze Peptid-Fragmente zurück, CLIP, die immer noch an MHC II gebunden sind. 7 Figure 5-10 part 2 of 2 Das endozytierte Antigen wird im Endosom ebenfalls zu Peptiden fragmentiert, CLIP-Peptide blockieren die Bindung der. Enjoy the videos and music you love, upload original content, and share it all with friends, family, and the world on YouTube MHC II molecules associate during their assembly in the ER with the invariant chain Ii that acts as a pseudopeptide by filling the MHC class II peptide-binding groove and in addition targets MHC. The role of the invariant chain (Ii), an MHC class II‐associated chaperone, in B cell development is controversial. Ii deficient mice (Ii-/- mice) show a defect in B cell development.This defect has been attributed to the absence of a fragment liberated from the Ii by intramembranous proteolysis. It was proposed that this fragment is required for activation of the NF‐κB pathway as a.
Regulation of Dendritic Cell Migration by CD74, the MHC Class II-Associated Invariant Chain. Gabrielle Faure-Andr é 1, *, Pablo Vargas 1, 2, *, Maria-Isabel Yuseff 1, Mélina Heuzé 1, Jheimmy Diaz 1, Danielle Lankar 1, Veronica Steri 1, Jeremy Manry 1, Stéphanie Hugues 1, Fulvia Vascotto 1, Jérôme Boulanger 3, Graça Raposo 3, Maria-Rosa Bono 2, 4, Mario Rosemblatt 2, 4, 5, Matthieu Piel. INVARIANT CHAIN CD 74 Non MHC encoded protein Interacts with class II molecule preventing any endogenously derived peptide from binding Also involved in the folding of class II α andβ chains, their exit from RER, and subsequent routing. 53. ASSEMBLY OF CLASS II MHC MOLECULE 54 The MHC class II-associated invariant chain behaves as a resident endoplasmic reticulum protein in the absence of class II molecules. In humans, two predominant forms exist; one, p35, differs from. Bidirectional binding of invariant chain peptides to an MHC class II molecule Sebastian Gunthera b'1, Andreas Schlundt3,1, Jana Sticht3, Yvette Roskeb# Udo Heinemannb, Karl-Heinz Wiesmullerc, Giinther Jungc, Kirsten Falkb# Olaf Rdtzschkebd, and Christian Freund3'2 aLeibniz-lnstitute for Molecular Pharmacology and Freie Universitat Berlin, 13125 Berlin, Germany; bMax-Delbruck-Center for.
Chaperones in ER; invariant chain in ER, Golgi and MHC Class II compartment/Class II vesicle; DM: End Result: Presentation of foreign-intracellular antigens or altered self-antigens; targets cell for destruction: Presentation of foreign extracellular antigens; induces antibody production, and attracts immune cells to area of infection: References and further reading: Cellular and Molecular. MHC II vaccines are MHC class I+ tumor cells that are transduced with costimulatory molecules and MHC II alleles syngeneic to the prospective recipient. Because the vaccine cells do not express the MHC II-associated invariant chain (Ii), we hypothesized that they will present endogenously synthesized tumor peptides that are not presented by professional Ii+ antigen presenting cells (APC) and. BACKGROUND: The invariant chain plays a crucial role in antigen presentation by influencing the expression and peptide loading of major histocompatibility complex (MHC) class II molecules. Therefore, coordinate expression of these molecules is important for antigen presentation. METHODS: Immunohistological studies were performed on frozen sections of many rat tissues in order to examine. Using data from nearly 400 GCs, we determined that EBVaGCs display high mRNA levels for virtually all MHC-II genes, as well as the MHC-II-like α- and β-chains, and the invariant chain encoded by. invariant chain MHC II in a raft-like membrane domain Julian T. Hauser and Robert Lindner1 Hannover Medical School, Department of Cell Biology, Center for Anatomy, Hannover, Germany RECEIVED JULY 1, 2013; REVISED MAY 8, 2014; ACCEPTED JUNE 28, 2014. DOI: 10.1189/jlb.2A0713-353R ABSTRACT The BCR binds antigen for processing and subsequent presentation on MHC II molecules. Polyvalent antigen.
Here, we show that HIV-1 Nef inhibits MHC II restricted peptide presentation to specific T cells and thus may affect the induction of antiviral immune responses. Nef mediates this effect by reducing the surface level of mature (i.e., peptide-loaded) MHC II while increasing levels of immature MHC II, which are functionally incompetent because of their association with the invariant chain. Nef. MHC II-Komplexe bewegen sich zunächst in das Endoplasmatischen Retikulum und sind dort mit der Invarianten Kette assoziiert. Letztere bildet mit einer weiteren Invarianten Kette ein Homotrimer. In diesem stabilisierten Zustand liegt der Komplex an calnexin gebunden vor und verlässt das ER. Durch Proteasen wird die Invariante Kette (class-II-associated invariant chain peptide-CLIP. Major histocompatibility complex (MHC) class II-associated invariant chain (Ii) plays a critical role in antigen presentation, forming MHC class II peptide complexes for the generation of CD4 + T cell responses. Preclinical studies evaluating the fusion of Ii to antigens encoded in vector delivery systems have shown that this strategy may enhance T cell immune responses to the encoded.
The invariant chain (Ii), or peptides derived from it, regu- late the formation, trafficking, and antigen-presenting functions of MHC class I1 a,@ complexes in several ways. Ii promotes efficient assembly of the MHC class I1 a,@ heterodimers [l] and induces folding of MHC class I1 molecules into a conformation which subsequently leads to high-affinity antigenic peptide binding [2-41. Ii also. MHC class II invariant chain-adjuvanted viral vectored vaccines enhances T cell responses in humans. / PEACHI Consortium. In: Science Translational Medicine, Vol. 12, No. 548, eaaz7715, 2020. Research output: Contribution to journal › Journal article › Research › peer-revie Second, class II molecules are synthesized with their peptide-binding site blocked by invariant chain (Ii), and they aquire the capacity to bind antigens only after Ii has been degraded in the compartments where peptides reside. MHC class II molecules present exogenously derived antigen to CD4+ T lymphocytes, which are usually T helper cells. CD4 interacts with non-polymorphic residues of MHC. The major histocompatibility complex (MHC) class II-associated invariant chain (Ii) is thought to act as a chaperone that assists class II during folding, assembly, and transport. To define more precisely the role of Ii chain in regulating class II function, we have investigated in detail the biosynthesis, transport, and intracellular distribution of class II molecules in splenocytes from mice.
The major histocompatibility class (MHC) II-invariant chain (Ii) complexes are transmembrane glycoproteins that play a central role in adaptive immunity [1, 2]. They are synthesized in the endoplasmic reticulum (ER) where the nascent MHC class II α and β chains associate with Ii trimers [3, 4]. Once fully assembled, the MHC class II-Ii complexes are transported to the late endosomal. Based on binding of invariant chain (Ii) to major histocompatibility complex (MHC) class II molecules to form complexes, Ii-segment hybrids, Ii-key structure linking an epitope, or Ii class II-associated invariant chain peptide (CLIP) replaced with an epitope were used to increase immune response. It is currently unknown whether the Ii-segment cytosolic and transmembrane domains bind to the. mhc class polypeptides derived invariant chain immunomodulatory polypeptides immunomodulatory Prior art date 1997-02-24 Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Abandoned Application number.
Invariant chain (Ii), also called CD74, plays an important role in antigen presentation of MHC II molecules. In the present study, we analyzed the role of Ii on the production of sMHC II molecules. We found that the amount of sMHC II molecules in serum was decreased in Ii-deficient mice compared to wild-type mice. sMHC II molecules were secreted from cells transfected with MHC II molecules and. Major histocompatibility complex (MHC) class II associated invariant chain is a chaperone of the mammalian MHC class II antigen presentation pathway. It is responsible for targeting the MHC class II dimer to the endocytic pathway, which allows for the loading of exogenous antigens onto the MHC class II receptor. Two genes showing significant sequence similarity to the mammalian invariant chain. Class II molecules of the major histocompatibility complex (MHC) are composed of two polymorphic glycoprotein chains (alpha and beta), that associate in the ER with a third, non‐polymorphic glycoprotein known as the invariant chain (Ii). We have examined the relationship between the intracellular transport and physico‐chemical characteristics of various combinations of murine alpha, beta. Invariant chain (Ii) has been shown to play a significant part in the assembly of MHC class II molecules. Ii also binds to MHC class I, although it is not known when this first occurs or whether it can affect class I assembly. Our examination of lysates of Ld-transfected T2 cells showed that Ii bound intracellularly to folded, but not to open, forms of MHC class I. Furthermore, addition of. invariant chain (Ii) (23). In endosomes, Ii is proteolyzed, leaving only a short fragment of Ii (residues 81-104) bound to the MHC molecule. This fragment, known as class II-associated invariant chain-derived peptide (CLIP), dissoci-ates, leaving the MHC molecule in the empty active state. CLIP dissociation in endosomes can be accelerated by
MHC class II-associated invariant chain (I-A/I-E), also known as Ia antigen-associated invariant chain, are single-pass type II membrane glycoproteins containing a single thyroglobulin type-I domain. They are critical components in the processing of MHC class II antigen through forming a stabilizing complex following the alpha/beta heterodimer synthesis, and orchestrating complex trafficking. MHC class II-associated invariant chain linkage of antigen dramatically improves cell-mediated immunity induced by adenovirus vaccines. Research output: Contribution to journal › Journal article › Research › peer-revie Viele übersetzte Beispielsätze mit invariant chain - Deutsch-Englisch Wörterbuch und Suchmaschine für Millionen von Deutsch-Übersetzungen
MHC class II and invariant chain form nonamers-or, according to recent studies, pentamers and heptamers-that traffic into an acidic endosomal compartment. Within this compartment, invariant chain is degraded down to class II invariant chain-associated peptide (CLIP), which occupies the peptide binding groove of the MHC class II molecule. HLA-DM, a non-classical MHC protein, catalyzes the. MHC class II molecules are transmembrane glycoprotein heterodimers of alpha and beta subunits. Newly synthesized MHC II molecules present in the endoplasmic reticulum bind to a chaperone protein called invariant (Ii) chain. The binding of Ii prevents the premature binding of self antigens to the nascent MHC molecules in the ER and also guides. MHC class II αβ dimers associate with the invariant chain (Ii) in the endoplasmic reticulum (ER), traffic through the Golgi apparatus and are delivered to the plasma membrane MHC II. MHC II dient zur Präsentation extrazellulärer Antigene. MHC II wird nur von bestimmten Zellen, z. B. von dendritischen Zellen, exprimiert. Die Peptid-Bindungstasche dieses Komplexes wird - solange er sich im ER befindet - durch eine invariant chain, ebenfalls ein Peptid, blockiert
View application images and datasheets for 658 anti MHC-class-II-associated-invariant-chain Antibody antibodies from 24 leading antibody suppliers, plus reviews and the top related antibodie the invariant chain (Ii), a chaperone known to transport MHC class II to MIICs, performs a similar function for CD70. CD70 was found to travel by default to the plasma membrane, whereas Ii coexpression directed it to late endosomes and/or lysosomes. In cells containing the MHC class II presentation pathway, CD70 localized to MIICs. This localization relied on Ii, since transport of CD70 from.
When class-II MHC molecules are synthesized within RER, three pairs of class-II αβ chains associated with a pre-assembled trimer of a protein called invariant chain (Li, CD74). This trimeric protein prevents any endogenously antigen to bind to the cleft. The invariant chain consists of sorting signals in its cytoplasmic tail Tumor Cells Transduced with the MHC Class II Transactivator and CD80 Activate Tumor-Specific CD4+ T Cells Whether or Not They Are Silenced for Invariant Chain James A. Thompson, 1Samudra K. Dissanayake, Bruce R. Ksander,2 Keith L. Knutson,3 Mary L. Disis,3 and Suzanne Ostrand-Rosenberg1 1Department of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland; 2The.
MHC-II molecules are formed in the endoplasmic reticulum with the help of the chaperone calnexin (4) and are held ready by the invariant chain (li); the complex is later fused with the HLA-DM (DM) (right lower inset in panel B). After passage of the li-loaded MHC-II-DM complex through the Golgi (5) into the late endosomes (6), the invariant chain is cleaved by acid proteases, leaving a. ability of MHC class II molecules to sort into the endocytic pathway has generally been attributed to the invariant chain glycoproteln. In this paper, we present evidence suggesting that lumenal sequence in the MHC class II molecule itself control the post-Goigi entry of class II into endosomes. Single amlno acid changes have been introduced into a highly conserved region of the class II β. molecule Invariant chain (Ii) and MHC class I molecules is known to occur, but the basis of the interaction is undetermined. Evidence is presented here that the CLIP region of Ii is involved in this interaction. A peptide encoding residues 91-99 of CLIP (MRMATPLLM) stabilised multiple MHC class I alleles, with the methionine residue at position 99 having a crucial role in binding to H2-Kb. In the processing pathway for extracellular antigens, synthesis of MHC class II and invariant chain (li) occurs in the____. A. Cytosol. B. Golgi apparatus. C. Endoplasmic reticulum. D. Ribosomes. E. Lysosomes. 5. The invariant chain____ the empty peptide-binding groove. After vesicle fusion, the invariant chain is____ and peptides can enter the MHC class II grove. A. Activates; Added. B.
The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been. MHC Class II and Invariant Chain in Fetal Tissues 475 to cells of the macrophage lineage but also apparent in epithelial cells. In fetal whole mount (EGA 7 weeks), both LN2 and LN3 staining was present in scattered cells in all the organs examined. Stained cells were ei-ther within hematolymphopoietic organs or existed as scattered single cells within the interstitium of organ parenchyma and. MHC-II-containing vesicles may also fuse with autophagosomes, allowing for cross presentation of endogenously-derived peptides . In acidic vesicles, Ii is degraded into a short fragment called the class II-associated invariant chain peptide (CLIP). If MHC-II fails to bind peptide in the endosome, it is degraded in the acidic environment. The SCOP classification for the Class II MHC-associated invariant chain ectoplasmic trimerization domain superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information
MHC class II molecules are only expressed on antigen presenting cells like monocytes, macrophages, dendritic cells, and B cells. The MHC class I molecule has two protein chains, a larger alpha chain which contains both a peptide binding groove and a transmembrane region which anchors the MHC class I molecule onto the cell surface MHC class II molecules (MHC II) acquire their peptides in endosomes and present these to the TcR on CD4+ T lymphocytes. They are vital for the generation of humoral immune responses. MHC II assembly in the ER and trafficking to endosomes is guided by a specialized MHC II chaperone termed the invariant chain (Ii). Ii self‐associates into a trimer in the ER, this provides a scaffold for the. Startseite Fachrepositorium » Bidirectional binding of invariant chain peptides to an MHC class II molecule. Bidirectional binding of invariant chain peptides to an MHC class II molecule; Bidirectional binding of invariant chain peptides to an MHC class II molecule Sticht, Jana Roske, Yvette Heinemann, Udo Wiesmüller, Karl-Heinz Jung, Günther Falk, Kirsten Rötzschke, Olaf Freund, Christian.
MHC class II molecules assemble in the endoplasmic reticulum in a chaperone-mediated fashion to form a nine-chain structure consisting of three alpha beta dimers associated with an invariant chain trimer. This complex is transported through the Golgi apparatus and into the endosomal system. The signal for endosomal targeting resides in the cytoplasmic tail of the invariant chain. Current. 61-80 to either LAMP1 to facilitate lysosomal targeting or to the MHC-II invariant chain (Ii) significantly increased the activation of Ag-specific CD4+ T cells in vivo. Immunization with VacV-Ii-GP 61-80 activated endogenous Ag-specific CD4+ T cells that formed memory and rapidly re-expanded following heterologous challenge. Notably, immunization of mice with VacV expressing an MHC-II. MHC class II-associated invariant chain/CLIP, MHC II-interacting Thyroglobulin type-1 Thyroglobulin type-1 superfamily; UniProtKB:Q9PVD9. InterPro 198: UniProtKB:A1L1X6. InterPro 198: UniProtKB:Q2YDR9. InterPro 198: Transcripts . Genome Browsers. UCSC NCBI Ensembl ZFIN. Type Name Length (nt) Analysis ; mRNA: cd74b-201. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form an heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL.