SREK1

Last update 08 May 2025

Basic Info

Synonyms

DKFZp564B176, Serine/arginine-rich-splicing regulatory protein 86, SFRS12

+ [7]

Introduction

Participates in the regulation of alternative splicing by modulating the activity of other splice facors. Inhibits the splicing activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of SFRS3 (By similarity).

100 Clinical Results associated with SREK1

100 Translational Medicine associated with SREK1

0 Patents (Medical) associated with SREK1

Literatures (Medical) associated with SREK1

17 Sep 2022·The Journal of Maternal-Fetal & Neonatal MedicineQ4 · MEDICINE

Proteomic profile of preeclampsia in the first trimester of pregnancy

Q4 · MEDICINE

Article

Author: Salazar-Ybarra, Rodolfo Amador ; Martínez-de-Villarreal, Laura Elia ; Jacobo-Baca, Guillermo ; Vázquez-Barragán, Miguel Ángel ; Torres-de-la-Cruz, Víctor ; Guzmán-López, Santos ; Guzmán-López, Abel ; Elizondo-Omaña, Rodrigo Enrique

OBJECTIVEPreeclampsia (PE) is a leading cause of pregnancy-associated maternal and neonatal morbidity and mortality. Detection of patients at risk before the clinical onset of PE is a priority. Proteomics have become a valuable tool for the discovery of new biomarkers; however, the understanding of the underlying mechanism is necessary. The aim of the study was to determine differences between proteomic serum profiles of PE and normotensive pregnancies using quantitative and qualitative approaches.STUDY DESIGNSerum samples from pregnant women were taken at 10-12 weeks of gestation with follow-up to determine PE development. Samples were analyzed using nano 2-D liquid chromatography UPLC and qTOF-MS/MS.RESULTSA total of 136 women were recruited, of which eight (5.9%) developed PE, and eight normotensive were randomly selected as a control group for comparison. A different profile was obtained between groups. Nine proteins showed quantitative differences with fold-change over 1.5: PRRC2C (217.02), HEATR5A (179.46), ATP6 (162.38), PRRC2B (83.09), RBM25 (5.36), NUP205 (3.38), HLA-I (2.27), ZC3H13 (2.15), and SREK1 (1.66); and two under 0.66: Importin-4 (0.55) and Cytochrome b (0.26). Using bilateral Fisher's exact test for the qualitative approach, LRRK1 had statistical significance (p = .044), while PRRC2B (p = .121), PRRC2C (p = .134), and NUP205 (p = .134) showed a tendency to be present in PE.CONCLUSIONThe found proteins have plausibility with the early pathophysiological events that have been associated with this pathology. Further studies should be performed to confirm these findings and elucidate their specific roles.

01 Jul 2020·BrainQ1 · MEDICINE

Pathogenic SREK1 decrease in Huntington’s disease lowers TAF1 mimicking X-linked dystonia parkinsonism

Q1 · MEDICINE

Article

Author: Cabrera, Jorge R ; Pintado, Belén ; García-Escudero, Ramón ; Domínguez, Verónica ; Lucas, José J ; Santos-Galindo, María ; Pérez-Álvarez, María J ; Hernández, Ivó H ; Sánchez-Martín, Manuel

AbstractHuntington’s disease and X-linked dystonia parkinsonism are two monogenic basal ganglia model diseases. Huntington’s disease is caused by a polyglutamine-encoding CAG repeat expansion in the Huntingtin (HTT) gene leading to several toxic interactions of both the expanded CAG-containing mRNA and the polyglutamine-containing protein, while X-linked dystonia parkinsonism is caused by a retrotransposon insertion in the TAF1 gene, which decreases expression of this core scaffold of the basal transcription factor complex TFIID. SRSF6 is an RNA-binding protein of the serine and arginine-rich (SR) protein family that interacts with expanded CAG mRNA and is sequestered into the characteristic polyglutamine-containing inclusion bodies of Huntington’s disease brains. Here we report decreased levels of the SRSF6 interactor and regulator SREK1—another SR protein involved in RNA processing—which includes TAF1 as one of its targets. This led us to hypothesize that Huntington’s disease and X-linked dystonia parkinsonism pathogeneses converge in TAF1 alteration. We show that diminishing SRSF6 through RNA interference in human neuroblastoma cells leads to a decrease in SREK1 levels, which, in turn, suffices to cause diminished TAF1 levels. We also observed decreased SREK1 and TAF1 levels in striatum of Huntington’s disease patients and transgenic model mice. We then generated mice with neuronal transgenic expression of SREK1 (TgSREK1 mice) that, interestingly, showed transcriptomic alterations complementary to those in Huntington’s disease mice. Most importantly, by combining Huntington’s disease and TgSREK1 mice we verify that SREK1 overexpression corrects TAF1 deficiency and attenuates striatal atrophy and motor phenotype of Huntington’s disease mice. Our results therefore demonstrate that altered RNA processing upon SREK1 dysregulation plays a key role in Huntington’s disease pathogenesis and pinpoint TAF1 as a likely general determinant of selective vulnerability of the striatum in multiple neurological disorders.

01 Jul 2010·RNA BiologyQ3 · BIOLOGY

Analysis of SRrp86-regulated alternative splicing

Q3 · BIOLOGY

Article

Author: Patton, James G. ; Solis, Amanda S.

Previous work led to the hypothesis that SRrp86, a related member of the SR protein superfamily, can interact with and modulate the activity of other SR proteins. Here, we sought to test this hypothesis by examining the effect of changing SRrp86 concentrations on overall alternative splicing patterns. SpliceArrays were used to examine 9,854 splicing events in wild-type cells, cells overexpressing SRrp86, and cells treated with siRNAs to knockdown SRrp86. From among the 500 splicing events exhibiting altered splicing under these conditions, the splicing of c-Jun and IκBβ were validated as being regulated by SRrp86 resulting in altered regulation of their downstream targets. In both cases, functionally distinct isoforms were generated that demonstrate the role SRrp86 plays in controlling alternative splicing.

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SREK1

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