author_facet Siemasko, Karyn
Skaggs, Brian J.
Kabak, Shara
Williamson, Edward
Brown, Bruce K.
Song, Wenxia
Clark, Marcus R.
Siemasko, Karyn
Skaggs, Brian J.
Kabak, Shara
Williamson, Edward
Brown, Bruce K.
Song, Wenxia
Clark, Marcus R.
author Siemasko, Karyn
Skaggs, Brian J.
Kabak, Shara
Williamson, Edward
Brown, Bruce K.
Song, Wenxia
Clark, Marcus R.
spellingShingle Siemasko, Karyn
Skaggs, Brian J.
Kabak, Shara
Williamson, Edward
Brown, Bruce K.
Song, Wenxia
Clark, Marcus R.
The Journal of Immunology
Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
Immunology
Immunology and Allergy
author_sort siemasko, karyn
spelling Siemasko, Karyn Skaggs, Brian J. Kabak, Shara Williamson, Edward Brown, Bruce K. Song, Wenxia Clark, Marcus R. 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.168.5.2127 <jats:title>Abstract</jats:title> <jats:p>Ags that cross-link the B cell Ag receptor are preferentially and rapidly delivered to the MHC class II-enriched compartment for processing into peptides and subsequent loading onto MHC class II. Proper sorting of Ag/receptor complexes requires the recruitment of Syk to the phosphorylated immunoreceptor tyrosine-based activation motif tyrosines of the B cell Ag receptor constituent Igα. We postulated that the Igα nonimmunoreceptor tyrosine-based activation motif tyrosines, Y176 and Y204, contributed to receptor trafficking. Igα(YΔF176,204)/Igβ receptors were targeted to late endosomes, but were excluded from the vesicle lumen and could not facilitate the presentation of Ag to T cells. Subsequent analysis demonstrated that phosphorylation of Y176/Y204 recruited the B cell linker protein, Vav, and Grb2. Reconstitution of Igα(YΔF176,204)/Igβ with the B cell linker protein rescued both receptor-facilitated Ag presentation and entry into the MHC class II-enriched compartment. Thus, aggregation accelerates receptor trafficking by recruiting two separate signaling modules required for transit through sequential checkpoints.</jats:p> Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα The Journal of Immunology
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title Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_unstemmed Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_full Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_fullStr Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_full_unstemmed Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_short Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_sort receptor-facilitated antigen presentation requires the recruitment of b cell linker protein to igα
topic Immunology
Immunology and Allergy
url http://dx.doi.org/10.4049/jimmunol.168.5.2127
publishDate 2002
physical 2127-2138
description <jats:title>Abstract</jats:title> <jats:p>Ags that cross-link the B cell Ag receptor are preferentially and rapidly delivered to the MHC class II-enriched compartment for processing into peptides and subsequent loading onto MHC class II. Proper sorting of Ag/receptor complexes requires the recruitment of Syk to the phosphorylated immunoreceptor tyrosine-based activation motif tyrosines of the B cell Ag receptor constituent Igα. We postulated that the Igα nonimmunoreceptor tyrosine-based activation motif tyrosines, Y176 and Y204, contributed to receptor trafficking. Igα(YΔF176,204)/Igβ receptors were targeted to late endosomes, but were excluded from the vesicle lumen and could not facilitate the presentation of Ag to T cells. Subsequent analysis demonstrated that phosphorylation of Y176/Y204 recruited the B cell linker protein, Vav, and Grb2. Reconstitution of Igα(YΔF176,204)/Igβ with the B cell linker protein rescued both receptor-facilitated Ag presentation and entry into the MHC class II-enriched compartment. Thus, aggregation accelerates receptor trafficking by recruiting two separate signaling modules required for transit through sequential checkpoints.</jats:p>
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author Siemasko, Karyn, Skaggs, Brian J., Kabak, Shara, Williamson, Edward, Brown, Bruce K., Song, Wenxia, Clark, Marcus R.
author_facet Siemasko, Karyn, Skaggs, Brian J., Kabak, Shara, Williamson, Edward, Brown, Bruce K., Song, Wenxia, Clark, Marcus R., Siemasko, Karyn, Skaggs, Brian J., Kabak, Shara, Williamson, Edward, Brown, Bruce K., Song, Wenxia, Clark, Marcus R.
author_sort siemasko, karyn
container_issue 5
container_start_page 2127
container_title The Journal of Immunology
container_volume 168
description <jats:title>Abstract</jats:title> <jats:p>Ags that cross-link the B cell Ag receptor are preferentially and rapidly delivered to the MHC class II-enriched compartment for processing into peptides and subsequent loading onto MHC class II. Proper sorting of Ag/receptor complexes requires the recruitment of Syk to the phosphorylated immunoreceptor tyrosine-based activation motif tyrosines of the B cell Ag receptor constituent Igα. We postulated that the Igα nonimmunoreceptor tyrosine-based activation motif tyrosines, Y176 and Y204, contributed to receptor trafficking. Igα(YΔF176,204)/Igβ receptors were targeted to late endosomes, but were excluded from the vesicle lumen and could not facilitate the presentation of Ag to T cells. Subsequent analysis demonstrated that phosphorylation of Y176/Y204 recruited the B cell linker protein, Vav, and Grb2. Reconstitution of Igα(YΔF176,204)/Igβ with the B cell linker protein rescued both receptor-facilitated Ag presentation and entry into the MHC class II-enriched compartment. Thus, aggregation accelerates receptor trafficking by recruiting two separate signaling modules required for transit through sequential checkpoints.</jats:p>
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spelling Siemasko, Karyn Skaggs, Brian J. Kabak, Shara Williamson, Edward Brown, Bruce K. Song, Wenxia Clark, Marcus R. 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.168.5.2127 <jats:title>Abstract</jats:title> <jats:p>Ags that cross-link the B cell Ag receptor are preferentially and rapidly delivered to the MHC class II-enriched compartment for processing into peptides and subsequent loading onto MHC class II. Proper sorting of Ag/receptor complexes requires the recruitment of Syk to the phosphorylated immunoreceptor tyrosine-based activation motif tyrosines of the B cell Ag receptor constituent Igα. We postulated that the Igα nonimmunoreceptor tyrosine-based activation motif tyrosines, Y176 and Y204, contributed to receptor trafficking. Igα(YΔF176,204)/Igβ receptors were targeted to late endosomes, but were excluded from the vesicle lumen and could not facilitate the presentation of Ag to T cells. Subsequent analysis demonstrated that phosphorylation of Y176/Y204 recruited the B cell linker protein, Vav, and Grb2. Reconstitution of Igα(YΔF176,204)/Igβ with the B cell linker protein rescued both receptor-facilitated Ag presentation and entry into the MHC class II-enriched compartment. Thus, aggregation accelerates receptor trafficking by recruiting two separate signaling modules required for transit through sequential checkpoints.</jats:p> Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα The Journal of Immunology
spellingShingle Siemasko, Karyn, Skaggs, Brian J., Kabak, Shara, Williamson, Edward, Brown, Bruce K., Song, Wenxia, Clark, Marcus R., The Journal of Immunology, Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα, Immunology, Immunology and Allergy
title Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_full Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_fullStr Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_full_unstemmed Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_short Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
title_sort receptor-facilitated antigen presentation requires the recruitment of b cell linker protein to igα
title_unstemmed Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα
topic Immunology, Immunology and Allergy
url http://dx.doi.org/10.4049/jimmunol.168.5.2127