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Fc receptor-γ subunits with both polar or non-polar amino acids at position of T22 are capable of restoring surface expression of the high-affinity IgE receptor and degranulation in γ subunit-deficient rat basophilic leukemia cells
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SYSNO ASEP 0390079 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Fc receptor-γ subunits with both polar or non-polar amino acids at position of T22 are capable of restoring surface expression of the high-affinity IgE receptor and degranulation in γ subunit-deficient rat basophilic leukemia cells Tvůrce(i) Rashid, A. (PK)
Housden, J.E. (GB)
Helm, B.A. (GB)
Dráber, Petr (UMG-J) RIDZdroj.dok. Molecular Immunology. - : Elsevier - ISSN 0161-5890
Roč. 53, č. 3 (2013), s. 270-273Poč.str. 4 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova allergy ; high-affinity IgE receptor ; plasma membrane ; transmembrane signaling ; 3-helix assembly model Vědní obor RIV EB - Genetika a molekulární biologie CEP LD12073 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA301/09/1826 GA ČR - Grantová agentura ČR GAP302/10/1759 GA ČR - Grantová agentura ČR GBP302/12/G101 GA ČR - Grantová agentura ČR 1M0506 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000310822500013 DOI 10.1016/j.molimm.2012.08.007 Anotace The high-affinity IgE receptor (FcɛRI) is formed by the IgE-binding α subunit, β subunit and γ subunits homodimer. All three subunits are required for proper expression of the receptor on the plasma membrane of mast cells and basophils. However, the exact molecular mechanism of inter-subunit interactions required for correct expression and function of the FcɛRI complex remains to be identified. A recent study suggested that polar aspartate at position 194 within the transmembrane domain of the α subunit could interact by hydrogen bonding with polar threonine at position 22 in the transmembrane domains of the γ subunits. To verify this, we used previously isolated rat basophilic leukemia (RBL)-2H3 variant cells deficient in the expression of the FcɛRI-γ subunit (FcR-γ), and transfected them with DNA vectors coding for FcR-γ of the wild-type or mutants in which T22 was substituted for nonpolar alanine (T22A mutant) or polar serine (T22S mutant). Analysis of the transfectants showed that both T22A and T22S mutants were capable to restore surface expression of the FcɛRI similar to wild-type FcR-γ. Furthermore, cells transfected with wild-type, T22A or T22S FcR-γ showed comparably enhanced FcɛRI-mediated degranulation. Our data indicate that substitution of FcR-γ T22 with non-polar amino acid does not interfere with surface expression of the FcɛRI and its signaling capacity. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2013
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