rdf:type |
|
lifeskim:mentions |
umls-concept:C0004561,
umls-concept:C0013126,
umls-concept:C0079904,
umls-concept:C0812385,
umls-concept:C0871261,
umls-concept:C1422243,
umls-concept:C1704259,
umls-concept:C1704632,
umls-concept:C1705987,
umls-concept:C1706817,
umls-concept:C1710082,
umls-concept:C2911692
|
pubmed:issue |
7
|
pubmed:dateCreated |
2011-7-5
|
pubmed:abstractText |
CIN85, an adaptor protein which binds the C-terminal domain of tyrosine phosphorylated Cbl and Cbl-b, has been thought to be involved in the internalization and subsequent degradation of receptors. However, its physiological function remains unclear. To determine its role in B cells, we used Mb1-cre to generate mice with a B cell-specific deletion of CIN85. These mice had impaired T cell-independent type II antibody responses in vivo and diminished IKK-? activation and cellular responses to B cell receptor (BCR) cross-linking in vitro. Introduction of a constitutively active IKK-? construct corrected the defective antibody responses as well as cellular responses in the mutant mice. Together, our results suggest that CIN85 links the BCR to IKK-? activation, thereby contributing to T cell-independent immune responses.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Ikbkb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Sh3kbp1 protein, mouse
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1540-9538
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
4
|
pubmed:volume |
208
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1447-57
|
pubmed:meshHeading |
pubmed-meshheading:21708930-Animals,
pubmed-meshheading:21708930-Antibody Formation,
pubmed-meshheading:21708930-B-Lymphocytes,
pubmed-meshheading:21708930-Base Sequence,
pubmed-meshheading:21708930-Cell Proliferation,
pubmed-meshheading:21708930-Cell Survival,
pubmed-meshheading:21708930-DNA Primers,
pubmed-meshheading:21708930-I-kappa B Kinase,
pubmed-meshheading:21708930-Mice,
pubmed-meshheading:21708930-Mice, Inbred BALB C,
pubmed-meshheading:21708930-Mice, Inbred C57BL,
pubmed-meshheading:21708930-Mice, Knockout,
pubmed-meshheading:21708930-Mice, Transgenic,
pubmed-meshheading:21708930-NF-kappa B,
pubmed-meshheading:21708930-Neoplasm Proteins,
pubmed-meshheading:21708930-Nerve Tissue Proteins,
pubmed-meshheading:21708930-Receptors, Antigen, B-Cell,
pubmed-meshheading:21708930-Signal Transduction,
pubmed-meshheading:21708930-T-Lymphocytes
|
pubmed:year |
2011
|
pubmed:articleTitle |
CIN85 drives B cell responses by linking BCR signals to the canonical NF-kappaB pathway.
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pubmed:affiliation |
Laboratory for Lymphocyte Differentiation, RIKEN Research Center for Allergy and Immunology, Turumi-ku, Kanagawa 230-0045, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|