Regulation of interleukin-21 receptor expression and its signal transduction by WSB-2. 2010

Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
Department of Immunology, Yamagata University Faculty of Medicine, 2-2-2 Iida-nishi, Yamagata 990-9585, Japan.

Interleukin-21 (IL-21) is a pleiotropic cytokine that regulates T-cell, B-cell, NK-cell, and myeloid-cell functions. IL-21 binds with its cognate receptor complex, which consists of the IL-21 receptor (IL-21R) and the common gamma chain (gammac) receptor subunit. We identified novel IL-21R-binding molecule, WD-40 repeats containing SOCS-box-2, WSB-2. WSB-2 associated with the membrane-proximal intracytoplasmic region of IL-21R, including box1 and box2. Overexpression study of WSB-2 showed the reduction of IL-21R expression and IL-21-induced signal transduction. On the other hand, small interfering RNA for WSB-2 enhanced the expression level of IL-21R and IL-21-induced STAT3 activation, indicating that WSB-2 negatively controls the receptor expression. This report provides the first evidence that WSB-2 is a regulator of IL-21R expression and IL-21-induced signal transduction.

UI MeSH Term Description Entries
D007378 Interleukins Soluble factors which stimulate growth-related activities of leukocytes as well as other cell types. They enhance cell proliferation and differentiation, DNA synthesis, secretion of other biologically active molecules and responses to immune and inflammatory stimuli. Interleukin
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D047468 Immunoprecipitation The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution. Co-Immunoprecipitation,Immune Precipitation,Co Immunoprecipitation,Co-Immunoprecipitations,Immune Precipitations,Precipitation, Immune,Precipitations, Immune
D047908 Intracellular Signaling Peptides and Proteins Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors. Intracellular Signaling Peptides,Intracellular Signaling Proteins,Peptides, Intracellular Signaling,Proteins, Intracellular Signaling,Signaling Peptides, Intracellular,Signaling Proteins, Intracellular
D050796 STAT3 Transcription Factor A signal transducer and activator of transcription that mediates cellular responses to INTERLEUKIN-6 family members. STAT3 is constitutively activated in a variety of TUMORS and is a major downstream transducer for the CYTOKINE RECEPTOR GP130. APRF Transcription Factor,Acute-Phase Response Factor,IL6-Response Factor,LIF-Response Factor,STAT3 Protein,STAT3a Transcription Factor,STAT3b Transcription Factor,Signal Transducer and Activator of Transcription 3,Stat3alpha Transcription Factor,Stat3beta Transcription Factor,Acute Phase Response Factor,IL6 Response Factor,LIF Response Factor,Response Factor, Acute-Phase,Transcription Factor, APRF,Transcription Factor, STAT3,Transcription Factor, STAT3a,Transcription Factor, STAT3b,Transcription Factor, Stat3alpha,Transcription Factor, Stat3beta
D050826 Suppressor of Cytokine Signaling Proteins A family of structurally related proteins that are induced by CYTOKINES and negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. SOCS proteins contain a central SH2 DOMAIN and a C-terminal region of homology known as the SOCS box. SOCS Proteins,Suppressors of Cytokine Signaling Proteins
D053738 Interleukin-21 Receptor alpha Subunit An interleukin-21 receptor subunit that combines with the INTERLEUKIN RECEPTOR COMMON GAMMA SUBUNIT to form a high affinity receptor for interleukin-21. It signals via interaction of its cytoplasmic domain with JANUS KINASES such as JANUS KINASE 1 and JANUS KINASE 3. IL-21 Receptor alpha Chain,Interleukin-21 Receptor alpha Chain,IL 21 Receptor alpha Chain,Interleukin 21 Receptor alpha Chain,Interleukin 21 Receptor alpha Subunit
D034741 RNA, Small Interfering Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions. RNA, Scan,Repeat-Associated siRNA,Scan RNA,Small Scan RNA,Trans-Acting siRNA,siRNA,siRNA, Repeat-Associated,siRNA, Trans-Acting,Short Hairpin RNA,Short Interfering RNA,Small Hairpin RNA,Small Interfering RNA,scnRNA,shRNA,tasiRNA,Hairpin RNA, Short,Hairpin RNA, Small,Interfering RNA, Short,Interfering RNA, Small,RNA, Short Hairpin,RNA, Short Interfering,RNA, Small Hairpin,RNA, Small Scan,Repeat Associated siRNA,Scan RNA, Small,Trans Acting siRNA,siRNA, Repeat Associated,siRNA, Trans Acting

Related Publications

Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
June 1986, Scandinavian journal of immunology,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
April 1995, Biochimica et biophysica acta,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
November 1997, European journal of immunology,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
November 1994, Trends in biochemical sciences,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
July 1995, Annals of the New York Academy of Sciences,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
January 1989, Cold Spring Harbor symposia on quantitative biology,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
January 2001, Journal of bioscience and bioengineering,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
February 1994, Journal of leukocyte biology,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
December 1998, Seikagaku. The Journal of Japanese Biochemical Society,
Hidetoshi Nara, and Tadashi Onoda, and Mizanur Rahman, and Akemi Araki, and Farha M Juliana, and Nobuyuki Tanaka, and Hironobu Asao
November 2000, Transplant immunology,
Copied contents to your clipboard!