Literature DB >> 9705073

Isolation of two functional retinoid X receptor subtypes from the Ixodid tick, Amblyomma americanum (L.).

X Guo1, Q Xu, M A Harmon, X Jin, V Laudet, D J Mangelsdorf, M J Palmer.   

Abstract

Retinoid X receptors (RXR) play a central role in a variety of nuclear signaling pathways in both vertebrates and invertebrates. Vertebrate RXRs are encoded by a multigene family whereas the insect RXR homologue, ultraspiracle (USP), is encoded by a single gene. To determine if acarines possess an RXR homologue similar to insect USPs, we isolated cDNAs encoding two distinct RXR genes, AamRXR1 and AamRXR2, from the ixodid tick, Amblyomma americanum (L.). The DNA binding domains share 95 and 87% identity, respectively, with DNA binding domains from insect USP and vertebrate RXR proteins. However, the ligand binding domains of the AamRXRs are more similar to vertebrate RXRs than to insect USP ligand binding domains (approximately 71 vs approximately 52%). Northern blot and RT-PCR analysis reveal both unique and overlapping patterns of AamRXR1 and AamRXR2 expression. Transactivation analysis show that both AamRXRs encode proteins which can form functional ecdysteroid receptors but are unlikely to bind retinoic acids.

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Year:  1998        PMID: 9705073     DOI: 10.1016/s0303-7207(98)00073-2

Source DB:  PubMed          Journal:  Mol Cell Endocrinol        ISSN: 0303-7207            Impact factor:   4.102


  9 in total

1.  Structural and functional characterization of a novel type of ligand-independent RXR-USP receptor.

Authors:  Thomas Iwema; Isabelle M L Billas; Yannick Beck; François Bonneton; Hélène Nierengarten; Arnaud Chaumot; Geoff Richards; Vincent Laudet; Dino Moras
Journal:  EMBO J       Date:  2007-08-02       Impact factor: 11.598

2.  Activation of a delayed-early gene encoding MHR3 by the ecdysone receptor heterodimer EcR-B1-USP-1 but not by EcR-B1-USP-2.

Authors:  Q Lan; K Hiruma; X Hu; M Jindra; L M Riddiford
Journal:  Mol Cell Biol       Date:  1999-07       Impact factor: 4.272

3.  The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation.

Authors:  G M Clayton; S Y Peak-Chew; R M Evans; J W Schwabe
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-06       Impact factor: 11.205

4.  The ecdysteroid receptor regulates salivary gland degeneration through apoptosis in Rhipicephalus haemaphysaloides.

Authors:  Xiaojuan Lu; Zhipeng Zhang; Dongqi Yuan; Yongzhi Zhou; Jie Cao; Houshuang Zhang; Itabajara da Silva Vaz; Jinlin Zhou
Journal:  Parasit Vectors       Date:  2021-12-20       Impact factor: 3.876

5.  Thyroid hormone receptor orthologues from invertebrate species with emphasis on Schistosoma mansoni.

Authors:  Wenjie Wu; Edward G Niles; Philip T LoVerde
Journal:  BMC Evol Biol       Date:  2007-08-29       Impact factor: 3.260

6.  Structure-based analysis of the ultraspiracle protein and docking studies of putative ligands.

Authors:  Souphatta Sasorith; Isabelle M L Billas; Thomas Iwema; Dino Moras; Jean-Marie Wurtz
Journal:  J Insect Sci       Date:  2002-12-03       Impact factor: 1.857

7.  Characterization of a novel RXR receptor in the salmon louse (Lepeophtheirus salmonis, Copepoda) regulating growth and female reproduction.

Authors:  Christiane Eichner; Sussie Dalvin; Rasmus Skern-Mauritzen; Ketil Malde; Heidi Kongshaug; Frank Nilsen
Journal:  BMC Genomics       Date:  2015-02-14       Impact factor: 3.969

8.  The retinoid X receptor from mud crab: new insights into its roles in ovarian development and related signaling pathway.

Authors:  Jie Gong; Chencui Huang; Ling Shu; Chenchang Bao; Huiyang Huang; Haihui Ye; Chaoshu Zeng; Shaojing Li
Journal:  Sci Rep       Date:  2016-03-24       Impact factor: 4.379

Review 9.  Quantitative Visions of Reality at the Tick-Host Interface: Biochemistry, Genomics, Proteomics, and Transcriptomics as Measures of Complete Inventories of the Tick Sialoverse.

Authors:  Ben J Mans
Journal:  Front Cell Infect Microbiol       Date:  2020-09-11       Impact factor: 5.293

  9 in total

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