scholarly journals Alternate Splicing

2020 ◽  
Author(s):  
Keyword(s):  
Alternate Splicing

Alternate Splicing of CD44 Messenger RNA in Prostate Cancer Growth

2009 ◽  
Author(s):  
Kenneth A. Iczkowski ◽  
Eric W. Robbins ◽  
Kui Yang ◽  
Alina Handorean ◽  
Yaqiong Tang
Keyword(s):  
Prostate Cancer ◽  
Messenger Rna ◽  
Cancer Growth ◽  
Alternate Splicing

scholarly journals A hobo Transgene That Encodes the P-Element Transposase in Drosophila melanogaster: Autoregulation and Cytotype Control of Transposase Activity

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 195-204 ◽  
Author(s):  
Michael J Simmons ◽  
Kevin J Haley ◽  
Craig D Grimes ◽  
John D Raymond ◽  
Jarad B Niemi
Keyword(s):  
Drosophila Melanogaster ◽  
Gonadal Dysgenesis ◽  
P Element ◽  
Hsp70 Gene ◽  
Alternate Splicing ◽  
Male And Female ◽  
P Elements ◽  
Male Germline ◽  
Female Germline ◽  
Transposase Expression

Abstract Drosophila were genetically transformed with a hobo transgene that contains a terminally truncated but otherwise complete P element fused to the promoter from the Drosophila hsp70 gene. Insertions of this H(hsp/CP) transgene on either of the major autosomes produced the P transposase in both the male and female germlines, but not in the soma. Heat-shock treatments significantly increased transposase activity in the female germline; in the male germline, these treatments had little effect. The transposase activity of two insertions of the H(hsp/CP) transgene was not significantly greater than their separate activities, and one insertion of this transgene reduced the transposase activity of P(ry+, Δ2-3)99B, a stable P transgene, in the germline as well as in the soma. These observations suggest that, through alternate splicing, the H(hsp/CP) transgene produces a repressor that feeds back negatively to regulate transposase expression or function in both the somatic and germline tissues. The H(hsp/CP) transgenes are able to induce gonadal dysgenesis when the transposase they encode has P-element targets to attack. However, this ability and the ability to induce P-element excisions are repressed by the P cytotype, a chromosomal/cytoplasmic state that regulates P elements in the germline.

Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes

1993 ◽  
Vol 13 (8) ◽  
pp. 4986-4998
Author(s):  
C Hall ◽  
W C Sin ◽  
M Teo ◽  
G J Michael ◽  
P Smith ◽  
...  
Keyword(s):  
Rat Brain ◽  
Brain Regions ◽  
Sh2 Domain ◽  
Trophic Factors ◽  
Splice Acceptor Site ◽  
Acceptor Site ◽  
Related Protein ◽  
Gtpase Activating Protein ◽  
Alternate Splicing ◽  
Pachytene Spermatocytes

n-Chimerin (alpha 1-chimerin) is a brain GTPase-activating protein (GAP) for the ras-related p21rac. We now report the occurrence of another form of chimerin, termed alpha 2-chimerin. This is the product of an alternately spliced transcript of the human n-chimerin gene encoding an N-terminal SH2 (src homology 2) domain in addition to the phorbol ester receptor and GAP domains. alpha 1- and alpha 2-chimerin mRNAs were expressed differently. In the rat brain, only alpha 1-chimerin mRNA was expressed in cerebellar Purkinje cells, although both alpha 1- and alpha 2-chimerin mRNAs occurred in neurons in the cerebral cortex, hippocampus, and thalamus. Only alpha 2-chimerin RNA was expressed in rat testes, in early pachytene spermatocytes. A 45-kDa SH2-containing chimerin corresponding to the alpha 2 form was purified from rat brain. As with Escherichia coli 45-kDa recombinant alpha 2-chimerin, purified brain alpha 2-chimerin exhibited racGAP activity which was stimulated by phosphatidylserine. The recombinant SH2 domain bound several 32P-labelled phosphoproteins of PC12 cells, whose phosphorylation increased in response to trophic factors, including nerve growth factor. To examine the relationships of alpha 1- and alpha 2-chimerin transcripts, human genomic DNA clones were characterized. In alpha 2-chimerin mRNA, a 3' splice acceptor site within exon 1 of alpha 1-chimerin mRNA was used, replacing its 5' untranslated region and N-terminal coding sequence. The single human n-chimerin gene was mapped to chromosome 2q31-q32.1, colocalizing with the CRE-BP1 transcription factor gene (2q32). It contained several splice junctions conserved with the sequence-related protein kinase C and bcr genes. alpha 2-Chimerin is only the second SH2-containing GAP and the first example of an SH2 domain generated by alternate splicing.

Reconstitution of human atlastin fusion activity reveals autoinhibition by the C terminus

2021 ◽  
Vol 221 (2) ◽  
Author(s):  
Daniel Crosby ◽  
Melissa R. Mikolaj ◽  
Sarah B. Nyenhuis ◽  
Samantha Bryce ◽  
Jenny E. Hinshaw ◽  
...  
Keyword(s):  
Network Formation ◽  
Fusion Activity ◽  
Amphipathic Helix ◽  
Alternate Splicing ◽  
Charge Reversal ◽  
Splice Isoforms ◽  
C Terminus ◽  
Splice Isoform ◽  
Inhibitory Domain ◽  
Α Helix

ER network formation depends on membrane fusion by the atlastin (ATL) GTPase. In humans, three paralogs are differentially expressed with divergent N- and C-terminal extensions, but their respective roles remain unknown. This is partly because, unlike Drosophila ATL, the fusion activity of human ATLs has not been reconstituted. Here, we report successful reconstitution of fusion activity by the human ATLs. Unexpectedly, the major splice isoforms of ATL1 and ATL2 are each autoinhibited, albeit to differing degrees. For the more strongly inhibited ATL2, autoinhibition mapped to a C-terminal α-helix is predicted to be continuous with an amphipathic helix required for fusion. Charge reversal of residues in the inhibitory domain strongly activated its fusion activity, and overexpression of this disinhibited version caused ER collapse. Neurons express an ATL2 splice isoform whose sequence differs in the inhibitory domain, and this form showed full fusion activity. These findings reveal autoinhibition and alternate splicing as regulators of atlastin-mediated ER fusion.

scholarly journals Sequence of the murine Huntington disease gene: evidence for conservation, alternate splicing and polymorphism in a triplet (CCG) repeat

1994 ◽  
Vol 3 (3) ◽  
pp. 530-530 ◽  
Author(s):  
B. Lin ◽  
J. Nasir ◽  
H. MacDonald ◽  
G. Hutchinson ◽  
R.K. Graham ◽  
...  
Keyword(s):  
Huntington Disease ◽  
Disease Gene ◽  
Alternate Splicing ◽  
Huntington Disease Gene

scholarly journals RET alternate splicing influences the interaction of activated RET with the SH2 and PTB domains of Shc, and the SH2 domain of Grb2

Oncogene ◽  
1997 ◽  
Vol 14 (7) ◽  
pp. 763-771 ◽  
Author(s):  
María Jesús Lorenzo ◽  
Gerald D Gish ◽  
Carol Houghton ◽  
Timothy J Stonehouse ◽  
Tony Pawson ◽  
...  
Keyword(s):  
Sh2 Domain ◽  
Alternate Splicing ◽  
Ptb Domains

scholarly journals Human Na+-myo-inositol cotransporter gene: alternate splicing generates diverse transcripts

1998 ◽  
Vol 274 (5) ◽  
pp. C1215-C1225 ◽  
Author(s):  
Francesca Porcellati ◽  
Tommy Hlaing ◽  
Masaki Togawa ◽  
Martin J. Stevens ◽  
Dennis D. Larkin ◽  
...  
Keyword(s):  
Molecular Level ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Transcriptional Unit ◽  
Cdna Sequencing ◽  
Alternate Splicing ◽  
Reading Frame ◽  
Hypertonic Stress ◽  
Exon Splicing

Na+- myo-inositol cotransport activity generally maintains millimolar intracellular concentrations of myo-inositol and specifically promotes transepithelial myo-inositol transport in kidney, intestine, retina, and choroid plexus. Glucose-induced, tissue-specific myo-inositol depletion and impaired Na+- myo-inositol cotransport activity are implicated in the pathogenesis of diabetic complications, a process modeled in vitro in cultured human retinal pigment epithelium (RPE) cells. To explore this process at the molecular level, a human RPE cDNA library was screened with a canine Na+-dependent myo-inositol cotransporter (SMIT) cDNA. Overlapping cDNAs spanning 3569 nt were cloned. The resulting cDNA sequence contained a 2154-nt open reading frame, 97% identical to the canine SMIT amino acid sequence. Genomic clones containing SMIT exons suggested that the cDNA is derived from at least five exons. Hypertonic stress induced a time-dependent increase, initially in a 16-kb transcript and subsequently in 11.5-, 9.8-, 8.5-, 3.8-, and ∼1.2-kb SMIT transcripts, that was ascribed to alternate exon splicing using exon-specific probes and direct cDNA sequencing. The human SMIT gene is a complex multiexon transcriptional unit that by alternate exon splicing generates multiple SMIT transcripts that accumulate differentially in response to hypertonic stress.

Proteomic and Sequence Analysis of Chicken Lens Crystallins Reveals Alternate Splicing and Translational Forms of βB2 and βA2 Crystallins

2004 ◽  
Vol 45 (8) ◽  
pp. 2705 ◽  
Author(s):  
Phillip A. Wilmarth ◽  
Jennifer R. Taube ◽  
Michael A. Riviere ◽  
Melinda K. Duncan ◽  
Larry L. David
Keyword(s):  
Sequence Analysis ◽  
Lens Crystallins ◽  
Alternate Splicing

Abstract 4724: DNA demethylation and double-strand breaks affect levels of theBRCA2Δ3 alternate splicing isoform

2020 ◽  
Author(s):  
Talia Ishfaq ◽  
Zaain Ahmad ◽  
Nourhan Mohamed ◽  
Milica Janosevic ◽  
Ziyad Abdelrahim ◽  
...  
Keyword(s):  
Dna Demethylation ◽  
Double Strand Breaks ◽  
Alternate Splicing ◽  
Strand Breaks
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