Alternative Initiation of Translation Accounts for a 67/45 kDa Dimorphism of the Human Estrogen Receptor ERα

Barraille, P; Chinestra, Patrick; Bayard, Françis; Faye, Jean-Charles

doi:10.1006/bbrc.1999.0334

Cited by 47 publications

(37 citation statements)

References 24 publications

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“…This mechanism for formation of multiple protein products from the same gene, while not common, has been observed with a variety of other eukaryotic genes (for example, see references in: Barraille et al 1999, O'Donovan & Baraban 1999, Liu et al 2000, Byrd et al 2002. Rat islet V52 and in vitro synthesized V52 co-migrate by SDS-PAGE and by 2-D NEPHGE/SDS-PAGE, suggesting that they are identical and that they are thus formed by the same mechanism of downstream translational initiation.…”

Section: Discussionmentioning

confidence: 54%

“…In the absence of an exon-intron structure amenable to minor splice variations, as in the mouse, utilization of alternate initiator codons provides a different means for modification of the cytoplasmic region of VIAAT in rat and human cells. Others have presented evidence that protein expression can be regulated in this manner and have proposed mechanisms (Barraille et al 1999, O'Donovan & Baraban 1999, Liu et al 2000, Byrd et al 2002.…”

Section: Discussionmentioning

confidence: 99%

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Identification and characterization of a novel isoform of the vesicular γ-aminobutyric acid transporter with glucose-regulated expression in rat islets

Suckow

Sweet

Yserloo

et al. 2006

Journal of Molecular Endocrinology

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Pancreatic islets are unique outside the nervous system in that they contain high levels of the inhibitory neurotransmitter -aminobutyric acid (GABA), synthesized by the enzyme glutamic acid decarboxylase (GAD). Since the role that GABA plays in the islet and the mechanisms whereby the two major GAD isoforms (GAD65 and GAD67) function as diabetes-associated autoantigens are unknown, continued characterization of the islet GAD-GABA system is important. We previously demonstrated that the GABA and glycine transporter vesicular inhibitory amino acid transporter (VIAAT also known as VGAT) is present in rat islets. Here we identify a novel 52 kDa variant of VIAAT in rat islets: VIAAT-52 (V52). V52 is an amino-terminally truncated form of VIAAT (V57) that likely results from utilization of a downstream start site of translation. V57 and V52 display different patterns of post-translational modification and cellular expression. Our results have indicated that islet content of V52, but not V57, is responsive to changes in glucose concentration and other extracellular conditions. VIAAT is expressed in the islet cells, but there have been conflicting findings regarding the presence of VIAAT in the cells. Here we have also provided additional evidence for the presence of VIAAT in islet cells and show that the cell line INS-1 expresses V57. V52 may be better adapted than V57 to the unique rat cell GAD-GABA system, which lacks GAD65 and in which VIAAT traffics to secretory granules rather than just to synaptic microvesicles.

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Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 99%

Identification and characterization of a novel isoform of the vesicular γ-aminobutyric acid transporter with glucose-regulated expression in rat islets

Suckow

Sweet

Yserloo

et al. 2006

Journal of Molecular Endocrinology

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“…ER␣-Neo(3) mRNA, which is identical to ER␣-⌬1 mRNA, would code for an isoform of ER␣ deleted for the A͞B domain (ER␣46). This latter isoform had been characterized at the mRNA and protein level in rat uterus and human cells (16,17,31,32). The N-terminal region of the full-length ER␣ harbors a ligandindependent transcriptional activation function AF-1 (33)(34)(35)(36).…”

Section: Discussionmentioning

confidence: 99%

The AF-1 activation-function of ERα may be dispensable to mediate the effect of estradiol on endothelial NO production in mice

Pendaries

Darblade

Rochaix

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

159

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Two isoforms of estrogen receptor (ER) have been described: ER␣ and ER␤. The initial gene targeting of ER␣, consisting in the introduction of a Neo cassette in exon 1 [␣ERKO, hereafter called ER␣-Neo KO (knockout)], was reported in 1993. More recently, another mouse deficient in ER␣ because of the deletion of exon 2 (ER␣KO, hereafter called ER␣-⌬2 KO) was generated. In ovariectomized ER␣-wild-type mice, estradiol (E2) increases uterine weight and basal production of endothelial nitric oxide (NO). Both of these effects are abolished in ER␣-⌬2 KO mice. In contrast, we show here that both of these effects of E 2 are partially (uterine weight) or totally (endothelial NO production) preserved in ER␣-Neo KO. We also confirm the presence of two ER␣ mRNA splice variants in uterus and aorta from ER␣-Neo KO mice. One of them encodes a chimeric ER␣ protein (ER␣55), partially deleted in the A͞B domain, that was detected in both uterus and aorta by Western blot analysis. The other ER␣ mRNA splice variant codes for an isoform deleted for the A͞B domain (ER␣46), which was detected in uterus of ER␣-Neo KO, and wild-type mice. This protein isoform was not detected in aorta. The identification of these two N-terminal modified isoforms in uterus, and at least one of them in aorta, probably explains the persistence of the E 2 effects in ER␣-Neo KO mice. Furthermore, ER␣-Neo KO mice may help in the elucidation of the specific functions of full-length ER␣ (ER␣66) and ER␣46, both shown to be physiologically generated in vivo.

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“…Most of these transcripts differ only in their 5'UTR (Untranslated Region) and will be mainly translated into a long form of ER, recognized as ER66 (Flouriot et al, 1998). However, a second form of ER protein, derived from alternative splicing of exon 1A mRNA or a site of alternative translation initiation (AUG codon 174) was discovered and named ER46 (Barrailler et al 1999;Flouriot et al, 2000). After translation, the 46 kDa isoform is truncated of the 173 first amino acids of the long form of 66 kDa.…”

Section: Er Structurementioning

confidence: 99%

Estrogens Involvement in the Physiopathology of Articular Cartilage

Moslemi¹,

Demoor²,

Boumediene³

et al. 2011

Challenges in Rheumatology

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Alternative Initiation of Translation Accounts for a 67/45 kDa Dimorphism of the Human Estrogen Receptor ERα

Cited by 47 publications

References 24 publications

Identification and characterization of a novel isoform of the vesicular γ-aminobutyric acid transporter with glucose-regulated expression in rat islets

Identification and characterization of a novel isoform of the vesicular γ-aminobutyric acid transporter with glucose-regulated expression in rat islets

The AF-1 activation-function of ERα may be dispensable to mediate the effect of estradiol on endothelial NO production in mice

Estrogens Involvement in the Physiopathology of Articular Cartilage

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