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Titolo:
Differential cellular compartmentalization of the nuclear receptor SpSHR2 splicing variants in early sea urchin embryos
Autore:
Kontrogianni-Konstantopoulos, A; Flytzanis, CN;
Indirizzi:
Univ Patras, Dept Biol, Patras 26500, Greece Univ Patras Patras Greece 26500 Patras, Dept Biol, Patras 26500, Greece Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Cellular Biol, Houston, TX 77030 USA
Titolo Testata:
MOLECULAR REPRODUCTION AND DEVELOPMENT
fascicolo: 2, volume: 60, anno: 2001,
pagine: 147 - 157
SICI:
1040-452X(200110)60:2<147:DCCOTN>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYROID-HORMONE RECEPTOR; RETINOIC ACID RECEPTORS; ORPHAN RECEPTOR; LOCALIZATION SIGNALS; RESPONSE ELEMENTS; COUP-TF; SUBCELLULAR-DISTRIBUTION; GLUCOCORTICOID RECEPTOR; TRANSCRIPTION FACTORS; STEROID-HORMONES;
Keywords:
SpSHR2; nuclear receptor; embryonic transcription factor; sea urchin embryo; subcellular localization; alternative splicing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Flytzanis, CN Univ Patras, Dept Biol, Patras 26500, Greece Univ Patras Patras Greece 26500 Biol, Patras 26500, Greece
Citazione:
A. Kontrogianni-Konstantopoulos e C.N. Flytzanis, "Differential cellular compartmentalization of the nuclear receptor SpSHR2 splicing variants in early sea urchin embryos", MOL REPROD, 60(2), 2001, pp. 147-157

Abstract

SpSHR2 is a member of the nuclear receptor superfamily, expressed in embryos, larvae, and adult tissues of sea urchin. During embryonic development, two receptor isoforms are produced via alternative splicing. One exhibits the typical structure of nuclear receptors (SpSHR2-full length), whereas theother is missing the entire LBD (SpSHR2-splice variant). DNA-constructs encoding these isoforms and two additional in vitro generated deletion mutants were engineered in an expression vector carrying the myc-tag. Expression of the tagged isoforms in S. purpuratus embryos showed that the exogenous SpSHR2 full-length protein displays a similar subcellular localization as the endogenous receptor. In early cleavage stages (4-cells), the full-length isoform is predominantly localized in the nucleus, whereas two cell divisions later (16-cells) protein accumulations are detected in both the nucleus and cytoplasm. To the contrary, the SpSHR2-splice variant is confined in the embryonic nuclei both at 4- and 16-cell stage embryos. Analysis of the intracellular distribution of two receptor mutants, one having a deletion within the DBD (DeltaP) and the other a truncation of the C-terminal F-domain (DeltaF), revealed that DeltaP is localized similarly to full-length receptor, whereas DeltaF is maintained in the nucleus, similar to the SpSHR2 splice variant. Investigation of the DNA binding and dimerization properties ofthe two SpSHR2 isoforms demonstrated that they recognize and bind to a DR1-elementas monomers, whereas DeltaP does not bind DNA and DeltaF binds to DR1 poorly. These results suggest that the receptor's putative LBD is responsible for the differential subcellular localization of the two natural SpSHR2-isoforms in early development. Mol. Reprod. Dev. 60: 147-157, 2001. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:42:43