scholarly journals The Syk-binding Ubiquitin Ligase c-Cbl Mediates Signaling-dependent B Cell Receptor Ubiquitination and B Cell Receptor-mediated Antigen Processing and Presentation

2012 ◽  
Vol 287 (20) ◽  
pp. 16636-16644 ◽  
Author(s):  
Bhuvana Katkere ◽  
Sarah Rosa ◽  
James R. Drake
Keyword(s):  
B Cell ◽  
Ubiquitin Ligase ◽  
Antigen Processing ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Antigen Processing And Presentation

scholarly journals Syk-dependent Actin Dynamics Regulate Endocytic Trafficking and Processing of Antigens Internalized through the B-Cell Receptor

2007 ◽  
Vol 18 (9) ◽  
pp. 3451-3462 ◽  
Author(s):  
Delphine Le Roux ◽  
Danielle Lankar ◽  
Maria-Isabel Yuseff ◽  
Fulvia Vascotto ◽  
Takeaki Yokozeki ◽  
...  
Keyword(s):  
B Cell ◽  
Antigen Processing ◽  
B Lymphocyte ◽  
Lymphocyte Activation ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Actin Dynamics ◽  
Endocytic Trafficking ◽  
Mhc Ii ◽  
Antigen Processing And Presentation

Antigen binding to the B-cell receptor (BCR) induces multiple signaling cascades that ultimately lead to B lymphocyte activation. In addition, the BCR regulates the key trafficking events that allow the antigen to reach endocytic compartments devoted to antigen processing, i.e., that are enriched for major histocompatibility factor class II (MHC II) and accessory molecules such as H2-DM. Here, we analyze the role in antigen processing and presentation of the tyrosine kinase Syk, which is activated upon BCR engagement. We show that convergence of MHC II- and H2-DM–containing compartments with the vesicles that transport BCR-uptaken antigens is impaired in cells lacking Syk activity. This defect in endocytic trafficking compromises the ability of Syk-deficient cells to form MHC II-peptide complexes from BCR-internalized antigens. Altered endocytic trafficking is associated to a failure of Syk-deficient cells to properly reorganize their actin cytoskeleton in response to BCR engagement. We propose that, by modulating the actin dynamics induced upon BCR stimulation, Syk regulates the positioning and transport of the vesicles that carry the molecules required for antigen processing and presentation.

scholarly journals Actin-Binding Protein 1 Regulates B Cell Receptor-Mediated Antigen Processing and Presentation in Response to B Cell Receptor Activation

2008 ◽  
Vol 180 (10) ◽  
pp. 6685-6695 ◽  
Author(s):  
Olusegun O. Onabajo ◽  
Margaret K. Seeley ◽  
Amruta Kale ◽  
Britta Qualmann ◽  
Michael Kessels ◽  
...  
Keyword(s):  
B Cell ◽  
Antigen Processing ◽  
Binding Protein ◽  
Cell Receptor ◽  
Receptor Activation ◽  
B Cell Receptor ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Antigen Processing And Presentation

scholarly journals Delivery of B Cell Receptor–internalized Antigen to Endosomes and Class II Vesicles

1997 ◽  
Vol 186 (8) ◽  
pp. 1299-1306 ◽  
Author(s):  
James R. Drake ◽  
Paul Webster ◽  
John C. Cambier ◽  
Ira Mellman
Keyword(s):  
B Cells ◽  
B Cell ◽  
Antigen Processing ◽  
Specific Antigen ◽  
Cell Receptor ◽  
Class Ii ◽  
Time Frame ◽  
B Cell Receptor ◽  
Subcellular Compartment ◽  
Endocytic Vesicles

B cell receptor (BCR)-mediated antigen processing is a mechanism that allows class II–restricted presentation of specific antigen by B cells at relatively low antigen concentrations. Although BCR-mediated antigen processing and class II peptide loading may occur within one or more endocytic compartments, the functions of these compartments and their relationships to endosomes and lysosomes remain uncertain. In murine B cells, at least one population of class II– containing endocytic vesicles (i.e., CIIV) has been identified and demonstrated to be distinct both physically and functionally from endosomes and lysosomes. We now demonstrate the delivery of BCR-internalized antigen to CIIV within the time frame during which BCR-mediated antigen processing and formation of peptide–class II complexes occurs. Only a fraction of the BCR-internalized antigen was delivered to CIIV, with the majority of internalized antigen being delivered to lysosomes that are largely class II negative. The extensive colocalization of BCR-internalized antigen and newly synthesized class II molecules in CIIV suggests that CIIV may represent a specialized subcellular compartment for BCR-mediated antigen processing. Additionally, we have identified a putative CIIV-marker protein, immunologically related to the Igα subunit of the BCR, which further illustrates the unique nature of these endocytic vesicles.

scholarly journals B Cell Receptor-Mediated Antigen Gathering Requires Ubiquitin Ligase Cbl and Adaptors Grb2 and Dok-3 to Recruit Dynein to the Signaling Microcluster

Immunity ◽  
2011 ◽  
Vol 34 (6) ◽  
pp. 905-918 ◽  
Author(s):  
Tim Schnyder ◽  
Angelo Castello ◽  
Christoph Feest ◽  
Naomi E. Harwood ◽  
Thomas Oellerich ◽  
...  
Keyword(s):  
B Cell ◽  
Ubiquitin Ligase ◽  
Cell Receptor ◽  
B Cell Receptor
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