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http://purl.uniprot.org/citations/23267015http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23267015http://www.w3.org/2000/01/rdf-schema#comment"Regulated intramembrane proteolysis is a central cellular process involved in signal transduction and membrane protein turnover. The presenilin homologue signal-peptide-peptidase-like 2a (SPPL2a) has been implicated in the cleavage of type 2 transmembrane proteins. We show that the invariant chain (li, CD74) of the major histocompatability class II complex (MHCII) undergoes intramembrane proteolysis mediated by SPPL2a. B lymphocytes of SPPL2a(-/-) mice accumulate an N-terminal fragment (NTF) of CD74, which severely impairs membrane traffic within the endocytic system and leads to an altered response to B cell receptor stimulation, reduced BAFF-R surface expression, and accumulation of MHCII in transitional developmental stage T1 B cells. This results in significant loss of B cell subsets beyond the T1 stage and disrupted humoral immune responses, which can be recovered by additional ablation of CD74. Hence, we provide evidence that regulation of CD74-NTF levels by SPPL2a is indispensable for B cell development and function by maintaining trafficking and integrity of MHCII-containing endosomes, highlighting SPPL2a as a promising pharmacological target for depleting and/or modulating B cells."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.org/dc/terms/identifier"doi:10.1084/jem.20121069"xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Saftig P."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Fluhrer R."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Schroder B."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Hermans-Borgmeyer I."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Engelke M."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Eskelinen E.L."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Dittmann K."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Wienands J."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Lullmann-Rauch R."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Schneppenheim J."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Dressel R."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/author"Huttl S."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/name"J Exp Med"xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/pages"41-58"xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/title"The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain."xsd:string
http://purl.uniprot.org/citations/23267015http://purl.uniprot.org/core/volume"210"xsd:string
http://purl.uniprot.org/citations/23267015http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23267015
http://purl.uniprot.org/citations/23267015http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23267015
http://purl.uniprot.org/uniprot/#_B0QZX1-mappedCitation-23267015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23267015
http://purl.uniprot.org/uniprot/#_P34902-mappedCitation-23267015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23267015
http://purl.uniprot.org/uniprot/#_B7ZMX3-mappedCitation-23267015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23267015