Relevant bibliographies by topics / Sin1 Isoforms

Academic literature on the topic 'Sin1 Isoforms'

Author: Grafiati
Published: 4 June 2021
Last updated: 19 February 2023

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Journal articles on the topic "Sin1 Isoforms"

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Yuan, Yuanyang, Bangfen Pan, Haipeng Sun, Guoqiang Chen, Bing Su, and Ying Huang. "Characterization of Sin1 Isoforms Reveals an mTOR-Dependent and Independent Function of Sin1γ." PLOS ONE 10, no. 8 (August 11, 2015): e0135017. http://dx.doi.org/10.1371/journal.pone.0135017.

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Pearce, Laura R., Xu Huang, Jérôme Boudeau, Rafał Pawłowski, Stephan Wullschleger, Maria Deak, Adel F. M. Ibrahim, Robert Gourlay, Mark A. Magnuson, and Dario R. Alessi. "Identification of Protor as a novel Rictor-binding component of mTOR complex-2." Biochemical Journal 405, no. 3 (July 13, 2007): 513–22. http://dx.doi.org/10.1042/bj20070540.

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The mTOR (mammalian target of rapamycin) protein kinase is an important regulator of cell growth. Two complexes of mTOR have been identified: complex 1, consisting of mTOR–Raptor (regulatory associated protein of mTOR)–mLST8 (termed mTORC1), and complex 2, comprising mTOR–Rictor (rapamycininsensitive companion of mTOR)–mLST8–Sin1 (termed mTORC2). mTORC1 phosphorylates the p70 ribosomal S6K (S6 kinase) at its hydrophobic motif (Thr389), whereas mTORC2 phosphorylates PKB (protein kinase B) at its hydrophobic motif (Ser473). In the present study, we report that widely expressed isoforms of unstudied proteins termed Protor-1 (protein observed with Rictor-1) and Protor-2 interact with Rictor and are components of mTORC2. We demonstrate that immunoprecipitation of Protor-1 or Protor-2 results in the co-immunoprecipitation of other mTORC2 subunits, but not Raptor, a specific component of mTORC1. We show that detergents such as Triton X-100 or n-octylglucoside dissociate mTOR and mLST8 from a complex of Protor-1, Sin1 and Rictor. We also provide evidence that Rictor regulates the expression of Protor-1, and that Protor-1 is not required for the assembly of other mTORC2 subunits into a complex. Protor-1 is a novel Rictor-binding subunit of mTORC2, but further work is required to establish its role.
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Pearce, Laura R., Eeva M. Sommer, Kei Sakamoto, Stephan Wullschleger, and Dario R. Alessi. "Protor-1 is required for efficient mTORC2-mediated activation of SGK1 in the kidney." Biochemical Journal 436, no. 1 (April 27, 2011): 169–79. http://dx.doi.org/10.1042/bj20102103.

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The mTOR (mammalian target of rapamycin) protein kinase is an important regulator of cell growth and is a key target for therapeutic intervention in cancer. Two complexes of mTOR have been identified: complex 1 (mTORC1), consisting of mTOR, Raptor (regulatory associated protein of mTOR) and mLST8 (mammalian lethal with SEC13 protein 8) and complex 2 (mTORC2) consisting of mTOR, Rictor (rapamycin-insensitive companion of mTOR), Sin1 (stress-activated protein kinase-interacting protein 1), mLST8 and Protor-1 or Protor-2. Both complexes phosphorylate the hydrophobic motifs of AGC kinase family members: mTORC1 phosphorylates S6K (S6 kinase), whereas mTORC2 regulates phosphorylation of Akt, PKCα (protein kinase Cα) and SGK1 (serum- and glucocorticoid-induced protein kinase 1). To investigate the roles of the Protor isoforms, we generated single as well as double Protor-1- and Protor-2-knockout mice and studied how activation of known mTORC2 substrates was affected. We observed that loss of Protor-1 and/or Protor-2 did not affect the expression of the other mTORC2 components, nor their ability to assemble into an active complex. Moreover, Protor knockout mice display no defects in the phosphorylation of Akt and PKCα at their hydrophobic or turn motifs. Strikingly, we observed that Protor-1 knockout mice displayed markedly reduced hydrophobic motif phosphorylation of SGK1 and its physiological substrate NDRG1 (N-Myc downregulated gene 1) in the kidney. Taken together, these results suggest that Protor-1 may play a role in enabling mTORC2 to efficiently activate SGK1, at least in the kidney.
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SINN, PATRICK L., and CURT D. SIGMUND. "Identification of three human renin mRNA isoforms from alternative tissue-specific transcriptional initiation." Physiological Genomics 3, no. 1 (June 29, 2000): 25–31. http://dx.doi.org/10.1152/physiolgenomics.2000.3.1.25.

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Sinn, Patrick L., and Curt D. Sigmund. Identification of three human renin mRNA isoforms from alternative tissue-specific transcriptional initiation. Physiol Genomics 3: 25–31, 2000.—We have reported that mice transgenic for 140- and 160-kb P1 phage artificial chromosomes (PACs) containing the human renin gene express the gene in a highly tissue-restricted and regulated manner. Herein, we demonstrate that the transgene is also expressed appropriately throughout development. In the course of this investigation, we identified the existence of three transcriptional isoforms of human renin mRNA derived from the utilization of alternative transcription start sites. The first isoform is the kidney-specific isoform, which utilizes the classic renin promoter. The second is a brain-specific isoform, which when previously identified in rats and mice was due to a transcription initiation site within intron A. However, the start site in the human gene resides ∼1,325 bp upstream of the classic promoter and encodes a new exon 1 (termed exon 1b) that splices directly to exon 2. The third isoform is lung specific and is due to transcriptional initiation 79 bp directly upstream of exon 2, fusing additional DNA within intron A (termed exon 1c) directly to exon 2 without splicing. Importantly, the alternative first exons observed in the PAC transgenic mice were identical to those used to transcribe renin in human fetal kidney, brain, and lung, suggesting these sites are bona fide isoforms of human renin mRNA and not artifacts of transgenesis. Moreover, the subtle differences in tissue-specific transcriptional initiation observed in the renin gene of rats and humans can be faithfully and accurately emulated in a transgenic model.
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Jin, Hyun Yong, Yanyan Tudor, Kaylee Choi, Zhifei Shao, Brian A. Sparling, Joseph G. McGivern, and Antony Symons. "High-Throughput Implementation of the NanoBRET Target Engagement Intracellular Kinase Assay to Reveal Differential Compound Engagement by SIK2/3 Isoforms." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 2 (December 18, 2019): 215–22. http://dx.doi.org/10.1177/2472555219893277.

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The real-time quantification of target engagement (TE) by small-molecule ligands in living cells remains technically challenging. Systematic quantification of such interactions in a high-throughput setting holds promise for identification of target-specific, potent small molecules within a pathophysiological and biologically relevant cellular context. The salt-inducible kinases (SIKs) belong to a subfamily of the AMP-activated protein kinase (AMPK) family and are composed of three isoforms in humans (SIK1, SIK2, and SIK3). They modulate the production of pro- and anti-inflammatory cytokines in immune cells. Although pan-SIK inhibitors are sufficient to reverse SIK-dependent inflammatory responses, the apparent toxicity associated with SIK3 inhibition suggests that isoform-specific inhibition is required to realize therapeutic benefit with acceptable safety margins. Here, we used the NanoBRET TE intracellular kinase assay, a sensitive energy transfer technique, to directly measure molecular proximity and quantify TE in HEK293T cells overexpressing SIK2 or SIK3. Our 384-well high-throughput screening of 530 compounds demonstrates that the NanoBRET TE intracellular kinase assay was sensitive and robust enough to reveal differential engagement of candidate compounds with the two SIK isoforms and further highlights the feasibility of high-throughput implementation of NanoBRET TE intracellular kinase assays for target-driven small-molecule screening.
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Chaubal, Ashlesha, Sokol V. Todi, and Lori A. Pile. "Inter-isoform-dependent Regulation of theDrosophilaMaster Transcriptional Regulator SIN3." Journal of Biological Chemistry 291, no. 22 (April 20, 2016): 11566–71. http://dx.doi.org/10.1074/jbc.c116.724799.

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Castel, Pau, Srisathiyanarayanan Dharmaiah, Matthew J. Sale, Simon Messing, Gabrielle Rizzuto, Antonio Cuevas-Navarro, Alice Cheng, et al. "RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity." Proceedings of the National Academy of Sciences 118, no. 33 (August 11, 2021): e2103261118. http://dx.doi.org/10.1073/pnas.2103261118.

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RAS proteins are molecular switches that interact with effector proteins when bound to guanosine triphosphate, stimulating downstream signaling in response to multiple stimuli. Although several canonical downstream effectors have been extensively studied and tested as potential targets for RAS-driven cancers, many of these remain poorly characterized. In this study, we undertook a biochemical and structural approach to further study the role of Sin1 as a RAS effector. Sin1 interacted predominantly with KRAS isoform 4A in cells through an atypical RAS-binding domain that we have characterized by X-ray crystallography. Despite the essential role of Sin1 in the assembly and activity of mTORC2, we find that the interaction with RAS is not required for these functions. Cells and mice expressing a mutant of Sin1 that is unable to bind RAS are proficient for activation and assembly of mTORC2. Our results suggest that Sin1 is a bona fide RAS effector that regulates downstream signaling in an mTORC2-independent manner.
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van Oevelen, Chris, Christopher Bowman, Jessica Pellegrino, Patrik Asp, Jemmie Cheng, Fabio Parisi, Mariann Micsinai, et al. "The Mammalian Sin3 Proteins Are Required for Muscle Development and Sarcomere Specification." Molecular and Cellular Biology 30, no. 24 (October 18, 2010): 5686–97. http://dx.doi.org/10.1128/mcb.00975-10.

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ABSTRACT The highly related mammalian Sin3A and Sin3B proteins provide a versatile platform for chromatin-modifying activities. Sin3-containing complexes play a role in gene repression through deacetylation of nucleosomes. Here, we explore a role for Sin3 in myogenesis by examining the phenotypes resulting from acute somatic deletion of both isoforms in vivo and from primary myotubes in vitro. Myotubes ablated for Sin3A alone, but not Sin3B, displayed gross defects in sarcomere structure that were considerably enhanced upon simultaneous ablation of both isoforms. Massively parallel sequencing of Sin3A- and Sin3B-bound genomic loci revealed a subset of target genes directly involved in sarcomere function that are positively regulated by Sin3A and Sin3B proteins. Both proteins were coordinately recruited to a substantial number of genes. Interestingly, depletion of Sin3B led to compensatory increases in Sin3A recruitment at certain target loci, but Sin3B was never found to compensate for Sin3A loss. Thus, our analyses describe a novel transcriptional role for Sin3A and Sin3B proteins associated with maintenance of differentiated muscle cells.
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Spain, Marla M., Joseph A. Caruso, Aishwarya Swaminathan, and Lori A. Pile. "Drosophila SIN3 Isoforms Interact with Distinct Proteins and Have Unique Biological Functions." Journal of Biological Chemistry 285, no. 35 (June 21, 2010): 27457–67. http://dx.doi.org/10.1074/jbc.m110.130245.

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Lozoya, Oswaldo A., Fuhua Xu, Dagoberto Grenet, Tianyuan Wang, Korey D. Stevanovic, Jesse D. Cushman, Thomas B. Hagler, et al. "A brain-specific pgc1α fusion transcript affects gene expression and behavioural outcomes in mice." Life Science Alliance 4, no. 12 (October 14, 2021): e202101122. http://dx.doi.org/10.26508/lsa.202101122.

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PGC1α is a transcriptional coactivator in peripheral tissues, but its function in the brain remains poorly understood. Various brain-specific Pgc1α isoforms have been reported in mice and humans, including two fusion transcripts (FTs) with non-coding repetitive sequences, but their function is unknown. The FTs initiate at a simple sequence repeat locus ∼570 Kb upstream from the reference promoter; one also includes a portion of a short interspersed nuclear element (SINE). Using publicly available genomics data, here we show that the SINE FT is the predominant form of Pgc1α in neurons. Furthermore, mutation of the SINE in mice leads to altered behavioural phenotypes and significant up-regulation of genes in the female, but not male, cerebellum. Surprisingly, these genes are largely involved in neurotransmission, having poor association with the classical mitochondrial or antioxidant programs. These data expand our knowledge on the role of Pgc1α in neuronal physiology and suggest that different isoforms may have distinct functions. They also highlight the need for further studies before modulating levels of Pgc1α in the brain for therapeutic purposes.
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Dissertations / Theses on the topic "Sin1 Isoforms"

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Cloonan, Nicole, and N/A. "Sin1 and Sin1 Isoforms: An Investigation into the Biological Significance of a Novel Human Protein Family." Griffith University. School of Biomolecular and Biomedical Science, 2006. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20071102.150237.

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Stress activated protein kinase (SAPK) interacting protein 1 (Sin1) is a member of a recently characterized gene family, conserved from yeast to humans. The gene copy number is strictly conserved (one Sin1 gene per genome), and the protein may be expressed ubiquitously in mammalian tissues. The Sin1 family has been implicated in several different signal transduction pathways. Originally identified as a partial cDNA and candidate Ras inhibitor, recent functional studies have revealed interactions with an interferon (IFN) receptor subunit (IFNAR2), and the SAPK JNK. Interactions have also been described between the yeast orthologues and the phosphatidylinositol kinase TOR2. Collectively, these data suggest that Sin1 has an important cellular role, and this study has investigated possible functions for this protein. As human Sin1 proteins have no paralogues within the genome, secondary structure homology was used to identify major domains within the protein. Four major domains within human Sin1 were deduced: an N-terminal domain containing a functional nuclear localization signal, a functional nuclear export signal, and a coiledcoil region; the conserved region in the middle that is likely to be a ubiquitin-like β-grasp protein binding domain; a Ras binding domain; and a pleckstrin homology-like domain that targets Sin1 to the plasma membrane and lipid rafts in vivo. Full and partial length EGFP constructs were used to examine the localization of human Sin1, and several isoforms derived from alternative splicing. All isoforms localized to the nucleus and nucleolus. Beyond this, Sin1α and Sin1ϒ had cytoplasmic staining, while Sin1 and Sin1β were also found at the plasma membrane and lipid rafts. Both the N-terminal domain and the conserved region in the middle were found to contribute to nuclear localization. Comparative genomic analysis between human, mouse, rat, dog, and chicken Sin1 genes revealed a number of conserved intronic regions, and the putative functions of these were predicted. Additionally, a putative promoter module within a CpG island and encompassing the transcription start site was predicted in all species. The human CpG island was found to have promoter activity in HEK293 cells. Using bioinformatics, genes that may be co-regulated with Sin1 were identified. These genes contained the Sin1 promoter module, and were found to co-express in large scale gene expression studies. Most of these genes were directly involved in the cellular response to pathogen infection, suggesting a conserved role for Sin1 in this pathway. Key biochemical functions of the Sin1 proteins were also identified, including the ability of Sin1 proteins to form dimers, and the ability of over-expressed Sin1 to induce apoptosis (mediated through the conserved region in the middle). Additionally, endogenous Sin1 protein levels were found to change following serum deprivation and hypoosmotic stress. Together, these studies have provided significant insight into the cellular role of Sin1, suggesting a role in inducing apoptosis as part of the IFN response to viral infection. The biological significance of the Sin1 proteins is discussed in the context of their predicted functions and the evolution of the protein family.
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Bartz, Michaela. "Interaktion der Na+, K+-ATPase mit Palytoxin und herzaktiven Steroiden an drei verschiedenen Isoformen der [alpha]-Untereinheit [Alpha-Untereinheit] sowie die Identifikation von Aminosäuren aus dem Ionophor der Na+, K+-ATPase, die kritisch für den Ionentransport und die Enzymfunktion sind." Giessen : VVB Laufersweiler, 2008. http://d-nb.info/98904758X/34.

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Bartz, Michaela. "Interaktion der Na+,K+-ATPase mit Palytoxin und herzaktiven Steroiden an drei verschiedenen Isoformen der [alpha]-Untereinheit [Alpha-Untereinheit] sowie die Identifikation von Aminosäuren aus dem Ionophor der Na+,K+-ATPase, die kritisch für den Ionentransport und die Enzymfunktion sind." Giessen VVB Laufersweiler, 2007. http://d-nb.info/988285185/04.

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Bartz, Michaela [Verfasser]. "Interaktion der Na+,K+-ATPase mit Palytoxin und herzaktiven Steroiden an drei verschiedenen Isoformen der α-Untereinheit [Alpha-Untereinheit] sowie die Identifikation von Aminosäuren aus dem Ionophor der Na+,K+-ATPase, die kritisch für den Ionentransport und die Enzymfunktion sind / eingereicht von Michaela Bartz." Giessen : VVB Laufersweiler, 2008. http://d-nb.info/98904758X/34.

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Conference papers on the topic "Sin1 Isoforms"

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Lewis, Monica J., Jianzhong Liu, and Douglas R. Hurst. "Abstract 2267: Defining roles of SIN3 isoforms in breast cancer metastasis." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2267.

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