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Titolo:
MIST functions through distinct domains in immunoreceptor signaling in thepresence and absence of LAT
Autore:
Goitsuka, R; Tatsuno, A; Ishiai, M; Kurosaki, T; Kitamura, D;
Indirizzi:
Sci Univ Tokyo, Res Inst Biol Sci, Div Mol Biol, Noda, Chiba 2780022, Japan Sci Univ Tokyo Noda Chiba Japan 2780022 Biol, Noda, Chiba 2780022, Japan Japan Sci Technol Corp, Precursory Res Embryon Sci & Technol, Inheritance & Variat Grp, Noda, Chiba 278, Japan Japan Sci Technol Corp Noda Chiba Japan 278 t Grp, Noda, Chiba 278, Japan Kansai Univ, Sch Med, Inst Hepatol, Div Mol Genet, Moriguchi, Osaka 5708506, Japan Kansai Univ Moriguchi Osaka Japan 5708506 Moriguchi, Osaka 5708506, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 276, anno: 2001,
pagine: 36043 - 36050
SICI:
0021-9258(20010921)276:38<36043:MFTDDI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ANTIGEN RECEPTOR; BRUTONS TYROSINE KINASE; ADAPTER PROTEIN SLP-76; T-CELL; PHOSPHOLIPASE C-GAMMA-2; MEDIATED ACTIVATION; B-CELLS; CATALYTIC ACTIVITY; MOLECULAR-CLONING; LINKER PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Goitsuka, R Sci Univ Tokyo, Res Inst Biol Sci, Div Mol Biol, 2669 Yamazaki, Noda, Chiba 2780022, Japan Sci Univ Tokyo 2669 Yamazaki Noda Chiba Japan 2780022 2, Japan
Citazione:
R. Goitsuka et al., "MIST functions through distinct domains in immunoreceptor signaling in thepresence and absence of LAT", J BIOL CHEM, 276(38), 2001, pp. 36043-36050

Abstract

MIST (also termed Clnk) is an adaptor protein structurally related to SLP-76 and BLNY./BASWSLP-65 hematopoietic cell-specific adaptor proteins. By using the BLNK-deficient DT40 chicken B cell system, we demonstrated MIST functions through distinct intramolecular domains in immunoreceptor signaling depending on the availability of linker for activation of T cells (LAT). MIST can partially restore the B cell antigen receptor (BCR) signaling in theBLNK-deficient cells, which requires phosphorylation of the two N-terminaltyrosine residues. Co-expression of LAT with MIST fully restored the BCR signaling and dispenses with the requirement of the two tyrosines in MIST for BCR signaling. However, some other tyrosine(s), as well as the Src homology (SH) 2 domain and the two proline-rich regions in MIST is still requiredfor full reconstitution of the BCR signaling, in cooperation with LAT. TheC-terminal proline-rich region of MIST is dispensable for the LAT-aided full restoration of MAP kinase activation, although it is responsible for theinteraction with LAT and for the localization in glycolipid-enriched microdomains. On the other hand, the N-terminal proline-rich region, which is a binding site of the SH3 domain of phospholipase Cy, is essential for BCR signaling. These results revealed a marked plasticity of MIST function as an adaptor in the cell contexts with or without LAT.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 09:54:39