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Artykuły w czasopismach na temat „STM1”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 3 lutego 2022

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1

Ligr, Martin, Iris Velten, Eleonore Fröhlich, Frank Madeo, Matthias Ledig, Kai-Uwe Fröhlich, Dieter H. Wolf, and Wolfgang Hilt. "The Proteasomal Substrate Stm1 Participates in Apoptosis-like Cell Death in Yeast." Molecular Biology of the Cell 12, no. 8 (August 2001): 2422–32. http://dx.doi.org/10.1091/mbc.12.8.2422.

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We have identified the yeast gene STM1 in an overexpression screen for new proteasomal substrates. Stm1 is unstable in wild-type cells and stabilized in cells with defective proteasomal activity and thus a bona fide substrate of the proteasome. It is localized in the perinuclear region and is required for growth in the presence of mutagens. Overexpression in cells with impaired proteasomal degradation leads to cell death accompanied with cytological markers of apoptosis: loss of plasma membrane asymmetry, chromatin condensation, and DNA cleavage. Cells lacking Stm1 display deficiency in the ap

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2

Barlow, Blake R., Lovreet S. Shergill, Mandy D. Bish, and Kevin W. Bradley. "Investigations of the Potential Interactions Between Pre-emergence Residual Herbicides, Variety, and Seed Treatments in Soybean." Weed Technology 32, no. 5 (September 24, 2018): 570–78. http://dx.doi.org/10.1017/wet.2018.44.

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AbstractField experiments were performed in 2016 and 2017 in Missouri to determine whether interactions exist between PRE herbicides and seed treatments in soybean. The experiments consisted of a randomized complete block design with factorial arrangements of varieties, seed treatments, and herbicides. We selected two genetically similar varieties of soybean, one with known tolerance to PPO-inhibiting herbicides and one with known sensitivity. Each variety of seed received three separate seed treatment mixtures (STMs): (1) STM1, imidacloprid plus prothioconazol+penflufen+metalaxyl plus metalax

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3

Bachtiar, Endang W., Kuo-Ching Sheng, Theodora Fifis, Anita Gamvrellis, Magdalena Plebanski, Peter J. Coloe, and Peter M. Smooker. "Delivery of a heterologous antigen by a registeredSalmonellavaccine (STM1)." FEMS Microbiology Letters 227, no. 2 (October 2003): 211–17. http://dx.doi.org/10.1016/s0378-1097(03)00683-9.

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4

Kumar, Chandrakesh, and Rajan Mishra. "Miniaturized Dual Band Meander Antenna For WLAN/STM1 Application." i-manager's Journal on Communication Engineering and Systems 4, no. 3 (July 15, 2015): 20–24. http://dx.doi.org/10.26634/jcs.4.3.3454.

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5

Balagopal, V., and R. Parker. "Stm1 modulates translation after 80S formation in Saccharomyces cerevisiae." RNA 17, no. 5 (April 1, 2011): 835–42. http://dx.doi.org/10.1261/rna.2677311.

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6

Balagopal, Vidya, and Roy Parker. "Stm1 Modulates mRNA Decay and Dhh1 Function in Saccharomyces cerevisiae." Genetics 181, no. 1 (November 17, 2008): 93–103. http://dx.doi.org/10.1534/genetics.108.092601.

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7

Hata, Hiroaki, Hisayuki Mitsui, Hong Liu, Yongli Bai, Clyde L. Denis, Yuki Shimizu, and Akira Sakai. "Dhh1p, a Putative RNA Helicase, Associates with the General Transcription Factors Pop2p and Ccr4p from Saccharomyces cerevisiae." Genetics 148, no. 2 (February 1, 1998): 571–79. http://dx.doi.org/10.1093/genetics/148.2.571.

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Abstract The POP2 (Caf1) protein in Saccharomyces cerevisiae affects a variety of transcriptional processes and is a component of the Ccr4p complex. We have isolated five multicopy suppressor genes of a pop2 deletion mutation: CCR4, DHH1 (a putative RNA helicase), PKC1, STM1, and MPT5 (multicopy suppressor of pop two). Overexpression of either the CCR4 or DHH1 genes effectively suppressed phenotypes associated with pop2 mutant cells; overexpression of PKC1, STM1, or MPT5 genes produced only partial suppression. Disruption of the CCR4 or DHH1 genes resulted in phenotypes similar to those observ

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8

Hayashi, Hikari, Riku Nagai, Taisho Abe, Miki Wada, Koichi Ito, and Nono Takeuchi-Tomita. "Tight interaction of eEF2 in the presence of Stm1 on ribosome." Journal of Biochemistry 163, no. 3 (October 23, 2017): 177–85. http://dx.doi.org/10.1093/jb/mvx070.

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9

Katayama, T., N. Inoue, and H. Torigoe. "Location of the triplex DNA-binding domain of Saccharomyces cerevisiae Stm1 protein." Nucleic Acids Symposium Series 51, no. 1 (November 1, 2007): 123–24. http://dx.doi.org/10.1093/nass/nrm062.

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10

Hayashi, N., and S. Murakami. "STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae." Molecular Genetics and Genomics 267, no. 6 (August 2002): 806–13. http://dx.doi.org/10.1007/s00438-002-0712-3.

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11

Katayama, T., and H. Torigoe. "The interaction between the purine motif triplex and the triplex DNA-binding domain of Saccharomyces cerevisiae Stm1 protein." Nucleic Acids Symposium Series 52, no. 1 (September 1, 2008): 111–12. http://dx.doi.org/10.1093/nass/nrn057.

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12

Kawano-Kawada, Miyuki, Taisuke Ueda, Hikari Mori, Haruka Ichimura, Kaoru Takegawa, and Takayuki Sekito. "Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe." Biochimica et Biophysica Acta (BBA) - Biomembranes 1863, no. 2 (February 2021): 183507. http://dx.doi.org/10.1016/j.bbamem.2020.183507.

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13

Chung, Kyung-Sook, Misun Won, Jung-Joon Lee, Jiwon Ahn, Kwang-Lae Hoe, Dong-Uk Kim, Kyung-Bin Song, and Hyang-Sook Yoo. "Yeast-based screening to identify modulators of G-protein signaling using uncontrolled cell division cycle by overexpression of Stm1." Journal of Biotechnology 129, no. 3 (May 2007): 547–54. http://dx.doi.org/10.1016/j.jbiotec.2007.01.007.

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14

Cortina, J. M., J. Martinell, V. Artiz, J. Fraile, and G. Rábago. "Comparative clinical results with Omniscience (STM1), Medtronic-Hall, and Björk-Shiley convexo-concave (70 degrees) prostheses in mitral valve replacement." Journal of Thoracic and Cardiovascular Surgery 91, no. 2 (February 1986): 174–83. http://dx.doi.org/10.1016/s0022-5223(19)36076-3.

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15

Nguyen, Thong Ba, Vishwanath Vasudev Prabhu, Yan Hong Piao, Young Eun Oh, Rami Fatima Zahra, and Young-Chul Chung. "Effects of Stathmin 1 Gene Knockout on Behaviors and Dopaminergic Markers in Mice Exposed to Social Defeat Stress." Brain Sciences 9, no. 9 (August 26, 2019): 215. http://dx.doi.org/10.3390/brainsci9090215.

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Stathmin (STMN), a microtubule-destabilizing factor, can regulate fear, anxiety, and learning. Social defeat stress (SDS) has detrimental effects on mental health and increases the risk of various psychiatric diseases. This study investigated the effects of STMN1 gene knockout (KO) on behavioral parameters and dopaminergic markers using an SDS mouse model. The STMN1 KO mice showed anxious hyperactivity, impaired object recognition, and decreased levels of neutral and social investigating behaviors at baseline compared to wild-type (WT) mice. The impact of SDS on neutral, social investigating a

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16

Yan, Kevin Kok-Phen, Ikenna Obi, and Nasim Sabouri. "The RGG domain in the C-terminus of the DEAD box helicases Dbp2 and Ded1 is necessary for G-quadruplex destabilization." Nucleic Acids Research 49, no. 14 (July 24, 2021): 8339–54. http://dx.doi.org/10.1093/nar/gkab620.

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Abstract The identification of G-quadruplex (G4) binding proteins and insights into their mechanism of action are important for understanding the regulatory functions of G4 structures. Here, we performed an unbiased affinity-purification assay coupled with mass spectrometry and identified 30 putative G4 binding proteins from the fission yeast Schizosaccharomyces pombe. Gene ontology analysis of the molecular functions enriched in this pull-down assay included mRNA binding, RNA helicase activity, and translation regulator activity. We focused this study on three of the identified proteins that

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17

Chung, Kyung-Sook, Misun Won, Sang-Bong Lee, Young-Joo Jang, Kwang-Lae Hoe, Dong-Uk Kim, Ji-Won Lee, Kyu-Won Kim та Hyang-Sook Yoo. "Isolation of a novel gene fromSchizosaccharomyces pombe: stm1 +, encoding a seven-transmembrane loop protein that may couple with the heterotrimeric Gα2 protein, Gpa2." Journal of Biological Chemistry 277, № 9 (березень 2002): 7626–27. http://dx.doi.org/10.1016/s0021-9258(19)82325-6.

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18

Chung, Kyung-Sook, Misun Won, Sang-Bong Lee, Young-Joo Jang, Kwang-Lae Hoe, Dong-Uk Kim, Ji-Won Lee, Kyu-Won Kim та Hyang-Sook Yoo. "Isolation of a Novel Gene fromSchizosaccharomyces pombe: stm1+Encoding a Seven-transmembrane Loop Protein That May Couple with the Heterotrimeric Gα2 Protein, Gpa2". Journal of Biological Chemistry 276, № 43 (18 липня 2001): 40190–201. http://dx.doi.org/10.1074/jbc.m100341200.

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19

GROVE-WHITE, D. H., A. J. H. LEATHERBARROW, P. J. CRIPPS, P. J. DIGGLE, and N. P. FRENCH. "Molecular epidemiology and genetic diversity ofCampylobacter jejuniin ruminants." Epidemiology and Infection 139, no. 11 (December 7, 2010): 1661–71. http://dx.doi.org/10.1017/s0950268810002736.

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SUMMARYMulti-locus sequence typing was performed on 1003Campylobacter jejuniisolates collected in a 2-year longitudinal study of 15 dairy farms and four sheep farms in Lancashire, UK. There was considerable farm-level variation in occurrence and prevalence of clonal complexes (CC). Clonal complexes ST61, ST21, ST403 and ST45 were most prevalent in cattle while in sheep CC ST42, ST21, ST48 and ST52 were most prevalent. CC ST45, a complex previously shown to be more common in summer months in human cases, was more prevalent in summer in our ruminant samples. Gene flow analysis demonstrated a hig

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20

Walsh, Ciara M., Michael Chvanov, Lee P. Haynes, Ole H. Petersen, Alexei V. Tepikin, and Robert D. Burgoyne. "Role of phosphoinositides in STIM1 dynamics and store-operated calcium entry." Biochemical Journal 425, no. 1 (December 14, 2009): 159–68. http://dx.doi.org/10.1042/bj20090884.

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Ca2+ entry through store-operated Ca2+ channels involves the interaction at ER–PM (endoplasmic reticulum–plasma membrane) junctions of STIM (stromal interaction molecule) and Orai. STIM proteins are sensors of the luminal ER Ca2+ concentration and, following depletion of ER Ca2+, they oligomerize and translocate to ER–PM junctions where they form STIM puncta. Direct binding to Orai proteins activates their Ca2+ channel function. It has been suggested that an additional interaction of the C-terminal polybasic domain of STIM1 with PM phosphoinositides could contribute to STIM1 puncta formation p

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21

Kubo, Takashi, Masayuki Hogiri, Hiroshi Kagata, and Atsushi Nakahira. "Synthesis of Nano-Sized Barium Titanate Powder by Rotary-Hydrothermal Process." Key Engineering Materials 421-422 (December 2009): 269–72. http://dx.doi.org/10.4028/www.scientific.net/kem.421-422.269.

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Nano-sized BaTiO3 powders with narrow size distribution and the high tetragonality were attempted to synthesize by the rotary-hydrothermal process in water system, using two kinds of commercial anatase-type TiO2 (ST21/ST01) with different particle size and Ba(OH)2. The rotary-hydrothermal syntheses were done with the rotary-speed of 20 revolutions per minute at 523 K for 24 h. Highly- and mono-dispersed BaTiO3 powders were successfully synthesized by applying the rotary-hydrothermal process. For rotary-hydrothermal synthesis, it was found that the average size, tetragonality, and quality of th

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22

Sato, Norihiro, Kiyomi Sasaki, Takuma Katayama, Yusuke Nomura, and Hidetaka Torigoe. "3B1446 Mechanism of the interaction between triplex DNA and triplex DNA-binding protein Stm1(3B Nucleic acid binding proteins,The 49th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 51, supplement (2011): S111—S112. http://dx.doi.org/10.2142/biophys.51.s111_6.

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23

Maloney, Jenny G., Yunah Jang, Aleksey Molokin, Nadja S. George, and Monica Santin. "Wide Genetic Diversity of Blastocystis in White-Tailed Deer (Odocoileus virginianus) from Maryland, USA." Microorganisms 9, no. 6 (June 21, 2021): 1343. http://dx.doi.org/10.3390/microorganisms9061343.

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Blastocystis is a gastrointestinal protist frequently reported in humans and animals worldwide. Wildlife populations, including deer, may serve as reservoirs of parasitic diseases for both humans and domestic animals, either through direct contact or through contamination of food or water resources. However, no studies of the occurrence and subtype distribution of Blastocystis in wildlife populations have been conducted in the United States. PCR and next generation amplicon sequencing were used to determine the occurrence and subtypes of Blastocystis in white-tailed deer (Odocoileus virginianu

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24

JONAS, R., S. KITTL, G. OVERESCH, and P. KUHNERT. "Genotypes and antibiotic resistance of bovineCampylobacterand their contribution to human campylobacteriosis." Epidemiology and Infection 143, no. 11 (December 16, 2014): 2373–80. http://dx.doi.org/10.1017/s0950268814003410.

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SUMMARYCampylobacter jejuniandCampylobacter coliare the most important bacterial causes of human gastroenteritis. Chicken has been recognized as a major source for human infection, whereas cattle might also contribute to a lesser extent. However, there is a paucity of information available regardingCampylobacterin Swiss cattle and their role for human campylobacteriosis. To gain more information on genotypes and antibiotic resistance of bovineC. jejuniandC. coliand on their contribution to human disease, 97 cattle isolates were analysed. Multilocus sequence typing (MLST) andflaBtyping were app

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25

Titze, Isabel, and Volker Krömker. "Antimicrobial Activity of a Phage Mixture and a Lactic Acid Bacterium against Staphylococcus aureus from Bovine Mastitis." Veterinary Sciences 7, no. 1 (March 6, 2020): 31. http://dx.doi.org/10.3390/vetsci7010031.

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The antimicrobial activity of a phage mixture and a lactic acid bacterium against Staphylococcus aureus isolates from bovine origin was investigated in vitro with regard to possible applications in the therapy of udder inflammation (mastitis) caused by bacterial infections. The S. aureus isolates used for inoculation derived from quarter foremilk samples of mastitis cases. For the examination of the antimicrobial activity, the reduction of the S. aureus germ density was determined [log10 cfu/mL]. The phage mixture consisted of the three obligatory lytic and S. aureus-specific phages STA1.ST29,

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Park, Ji Hee, Seung Yeon Jeong, Jun Hee Choi, and Eun Hui Lee. "Pathological Mechanism of a Constitutively Active Form of Stromal Interaction Molecule 1 in Skeletal Muscle." Biomolecules 11, no. 8 (July 21, 2021): 1064. http://dx.doi.org/10.3390/biom11081064.

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Stromal interaction molecule 1 (STIM1) is the main protein that, along with Orai1, mediates store-operated Ca2+ entry (SOCE) in skeletal muscle. Abnormal SOCE due to mutations in STIM1 is one of the causes of human skeletal muscle diseases. STIM1-R304Q (a constitutively active form of STIM1) has been found in human patients with skeletal muscle phenotypes such as muscle weakness, myalgia, muscle stiffness, and contracture. However, the pathological mechanism(s) of STIM1-R304Q in skeletal muscle have not been well studied. To examine the pathological mechanism(s) of STIM1-R304Q in skeletal musc

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Titze, Isabel, Tatiana Lehnherr, Hansjörg Lehnherr, and Volker Krömker. "Efficacy of Bacteriophages Against Staphylococcus aureus Isolates from Bovine Mastitis." Pharmaceuticals 13, no. 3 (February 26, 2020): 35. http://dx.doi.org/10.3390/ph13030035.

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The lytic efficacy of bacteriophages against Staphylococcus aureus isolates from bovine milk was investigated in vitro, regarding possible applications in the therapy of udder inflammation caused by bacterial infections (mastitis). The host range of sequenced, lytic bacteriophages was determined against a collection of 92 Staphylococcus (S.) aureus isolates. The isolates originated from quarter foremilk samples of clinical and subclinical mastitis cases. A spot test and a subsequent plaque assay were used to determine the phage host range. According to their host range, propagation and storage

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Li, Yong-jun, Lia Danelishvili, Dirk Wagner, Mary Petrofsky, and Luiz E. Bermudez. "Identification of virulence determinants of Mycobacterium avium that impact on the ability to resist host killing mechanisms." Journal of Medical Microbiology 59, no. 1 (January 1, 2010): 8–16. http://dx.doi.org/10.1099/jmm.0.012864-0.

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Mycobacterium avium is an opportunistic pathogen associated with pulmonary disease in non-AIDS patients and disseminated infection in patients with AIDS. The chief route of infection is by colonization and invasion of the mucosa of the gastrointestinal tract, but infection through the respiratory route also occurs. After crossing the mucosa, M. avium infects and replicates within tissue macrophages. To identify M. avium genes required for survival in vivo, a library of signature-tagged transposon mutants was constructed and screened for clones attenuated in mice. Thirty-two clones were found t

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Zhang, Lane, Limin Wang, Shu Li, Jingyi Xue, and Dali Luo. "Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhibiting STIM1 Aggregation." Cellular Physiology and Biochemistry 38, no. 6 (2016): 2183–93. http://dx.doi.org/10.1159/000445574.

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Background/Aims: Stromal interacting molecule-1 (STIM1) aggregation and redistribution to plasma membrane to interact with Orai1 constitute the core mechanism of store-operated Ca2+ entry (SOCE). Previous study has revealed that calsequestrin-1 (CSQ1) regulates SOCE in HEK293 cells through interacting with STIM1 and inhibiting STIM1/Orai1 interaction. Here, we further investigate how CSQ1/STIM1 interaction affects SOCE. Methods: Using confocal microscopy, STIM1 aggregation and co-localizations with CSQ1 or Orai1 upon Ca2+ store depletion by thapsigargin were measured and quantified by Imaris s

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Maus, Mate, Amit Jairaman, Peter B. Stathopulos, Martin Muik, Marc Fahrner, Carl Weidinger, Melina Benson, et al. "Missense mutation in immunodeficient patients shows the multifunctional roles of coiled-coil domain 3 (CC3) in STIM1 activation." Proceedings of the National Academy of Sciences 112, no. 19 (April 27, 2015): 6206–11. http://dx.doi.org/10.1073/pnas.1418852112.

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Store-operated Ca2+ entry (SOCE) is a universal Ca2+ influx pathway that is important for the function of many cell types. SOCE occurs upon depletion of endoplasmic reticulum (ER) Ca2+ stores and relies on a complex molecular interplay between the plasma membrane (PM) Ca2+ channel ORAI1 and the ER Ca2+ sensor stromal interaction molecule (STIM) 1. Patients with null mutations in ORAI1 or STIM1 genes present with severe combined immunodeficiency (SCID)-like disease. Here, we describe the molecular mechanisms by which a loss-of-function STIM1 mutation (R429C) in human patients abolishes SOCE. R4

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Jha, Archana, Malini Ahuja, József Maléth, Claudia M. Moreno, Joseph P. Yuan, Min Seuk Kim, and Shmuel Muallem. "The STIM1 CTID domain determines access of SARAF to SOAR to regulate Orai1 channel function." Journal of Cell Biology 202, no. 1 (July 1, 2013): 71–79. http://dx.doi.org/10.1083/jcb.201301148.

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Ca2+ influx by store-operated Ca2+ channels (SOCs) mediates all Ca2+-dependent cell functions, but excess Ca2+ influx is highly toxic. The molecular components of SOC are the pore-forming Orai1 channel and the endoplasmic reticulum Ca2+ sensor STIM1. Slow Ca2+-dependent inactivation (SCDI) of Orai1 guards against cell damage, but its molecular mechanism is unknown. Here, we used homology modeling to identify a conserved STIM1(448–530) C-terminal inhibitory domain (CTID), whose deletion resulted in spontaneous clustering of STIM1 and full activation of Orai1 in the absence of store depletion. C

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Dong-Sin, HOU, WANG Lin-Ci, and SIE Cing-Cun. "STME." Industrial Robot Magazine 4, no. 1 (January 31, 2015): 1–3. http://dx.doi.org/10.32738/irm.201501.0001.

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Commelin, M. "STMI." Revue Générale Nucléaire, no. 4 (July 1990): 418–19. http://dx.doi.org/10.1051/rgn/19904418.

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Yu, Junwei, Haining Zhang, Mingshu Zhang, Yongqiang Deng, Huiyu Wang, Jingze Lu, Tao Xu, and Pingyong Xu. "An aromatic amino acid in the coiled-coil 1 domain plays a crucial role in the auto-inhibitory mechanism of STIM1." Biochemical Journal 454, no. 3 (August 29, 2013): 401–9. http://dx.doi.org/10.1042/bj20130292.

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STIM1 (stromal interaction molecule 1) is one of the key elements that mediate store-operated Ca2+ entry via CRAC (Ca2+- release-activated Ca2+) channels in immune and non-excitable cells. Under physiological conditions, the intramolecular auto-inhibitions in STIM1 C- and STIM1 N-termini play essential roles in keeping STIM1 in an inactive state. However, the auto-inhibitory mechanism of the STIM1 C-terminus is still unclear. In the present study, we first predicted a short inhibitory domain (residues 310–317) in human STIM1 that might determine the different localizations of human STIM1 from

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Nomura, Atsuo, Shunichi Yokoe, Kiichiro Tomoda, Takatoshi Nakagawa, Francisco Javier Martin-Romero, and Michio Asahi. "Fluctuation in O-GlcNAcylation inactivates STIM1 to reduce store-operated calcium ion entry via down-regulation of Ser621 phosphorylation." Journal of Biological Chemistry 295, no. 50 (October 6, 2020): 17071–82. http://dx.doi.org/10.1074/jbc.ra120.014271.

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Stromal interaction molecule 1 (STIM1) plays a pivotal role in store-operated Ca2+ entry (SOCE), an essential mechanism in cellular calcium signaling and in maintaining cellular calcium balance. Because O-GlcNAcylation plays pivotal roles in various cellular function, we examined the effect of fluctuation in STIM1 O-GlcNAcylation on SOCE activity. We found that both increase and decrease in STIM1 O-GlcNAcylation impaired SOCE activity. To determine the molecular basis, we established STIM1-knockout HEK293 (STIM1-KO-HEK) cells using the CRISPR/Cas9 system and transfected STIM1 WT (STIM1-KO-WT-H

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Rao, Jaladanki N., Navneeta Rathor, Tongtong Zou, Lan Liu, Lan Xiao, Ting-Xi Yu, Yu-Hong Cui, and Jian-Ying Wang. "STIM1 translocation to the plasma membrane enhances intestinal epithelial restitution by inducing TRPC1-mediated Ca2+ signaling after wounding." American Journal of Physiology-Cell Physiology 299, no. 3 (September 2010): C579—C588. http://dx.doi.org/10.1152/ajpcell.00066.2010.

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Early epithelial restitution is an important repair modality in the gut mucosa and occurs as a consequence of epithelial cell migration. Canonical transient receptor potential-1 (TRPC1) functions as a store-operated Ca2+ channel (SOCs) in intestinal epithelial cells (IECs) and regulates intestinal restitution, but the exact upstream signals initiating TRPC1 activation after mucosal injury remain elusive. Stromal interaction molecule 1 (STIM1) is a single membrane-spanning protein and is recently identified as essential components of SOC activation. The current study was performed to determine

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Pascual-Caro, Carlos, Maria Berrocal, Aida M. Lopez-Guerrero, Alberto Alvarez-Barrientos, Eulalia Pozo-Guisado, Carlos Gutierrez-Merino, Ana M. Mata, and Francisco Javier Martin-Romero. "STIM1 deficiency is linked to Alzheimer’s disease and triggers cell death in SH-SY5Y cells by upregulation of L-type voltage-operated Ca2+ entry." Journal of Molecular Medicine 96, no. 10 (August 7, 2018): 1061–79. http://dx.doi.org/10.1007/s00109-018-1677-y.

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Abstract STIM1 is an endoplasmic reticulum protein with a role in Ca2+ mobilization and signaling. As a sensor of intraluminal Ca2+ levels, STIM1 modulates plasma membrane Ca2+ channels to regulate Ca2+ entry. In neuroblastoma SH-SY5Y cells and in familial Alzheimer’s disease patient skin fibroblasts, STIM1 is cleaved at the transmembrane domain by the presenilin-1-associated γ-secretase, leading to dysregulation of Ca2+ homeostasis. In this report, we investigated expression levels of STIM1 in brain tissues (medium frontal gyrus) of pathologically confirmed Alzheimer’s disease patients, and o

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Gu, J., A. Y. S. Law, B. H. Y. Yeung, and Chris K. C. Wong. "Characterization of stanniocalcin 1 binding and signaling in gill cells of Japanese eels." Journal of Molecular Endocrinology 54, no. 3 (June 2015): 305–14. http://dx.doi.org/10.1530/jme-14-0320.

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Stanniocalcin 1 (STC1) is a hypocalcemic hormone that is known to play an important role in calcium metabolism in teleost fish. An increase in blood Ca2+ levels stimulates its synthesis and release. The biological action of STC1 inhibits gill Ca2+ transport (GCAT), but we as yet have no clear understanding of how STC1 inhibits GCAT. In the present study, we characterized the binding, signaling, and action of STC1 on gill cells. Treatment of gill cell cultures with the extracts of corpuscles of Stannius or recombinant STC1 proteins (STC1–V5) led to an increase in cytosolic cAMP levels. Using in

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Covington, Elizabeth D., Minnie M. Wu, and Richard S. Lewis. "Essential Role for the CRAC Activation Domain in Store-dependent Oligomerization of STIM1." Molecular Biology of the Cell 21, no. 11 (June 2010): 1897–907. http://dx.doi.org/10.1091/mbc.e10-02-0145.

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Oligomerization of the ER Ca2+ sensor STIM1 is an essential step in store-operated Ca2+ entry. The lumenal EF-hand and SAM domains of STIM1 are believed to initiate oligomerization after Ca2+ store depletion, but the contributions of STIM1 cytosolic domains (coiled-coil 1, CC1; coiled-coil 2, CC2; CRAC activation domain, CAD) to this process are not well understood. By applying coimmunoprecipitation and fluorescence photobleaching and energy transfer techniques to truncated and mutant STIM1 proteins, we find that STIM1 cytosolic domains play distinct roles in forming both “resting” oligomers i

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Yang, Yanfang, Zhansheng Jiang, Ning Ma, Bin Wang, Jun Liu, Lina Zhang, and Lin Gu. "MicroRNA-223 Targeting STIM1 Inhibits the Biological Behavior of Breast Cancer." Cellular Physiology and Biochemistry 45, no. 2 (2018): 856–66. http://dx.doi.org/10.1159/000487180.

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Background/Aims: To investigate the cellular effects and clinical significance of microRNA-223 (miR-223) in breast cancer by targeting stromal interaction molecule1 (STIM1). Methods: Breast cancer cell lines (T47D, MCF-7, SKB-R3, MDA-MB-231 and MDA-MB-435) and a normal breast epithelial cell line (MCF-10A) were prepared for this study. MiR-223 mimics, anti-miR-223 and pcDNA 3.1-STIM1 were transiently transfected into cancer cells independently or together, and then RT-qPCR was performed to detect the expressions of miR-223 and STIM1 mRNA, dual-luciferase reporter assay was conducted to examine

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Jiang, WQ, AC Chang, M. Satoh, Y. Furuichi, PP Tam, and RR Reddel. "The distribution of stanniocalcin 1 protein in fetal mouse tissues suggests a role in bone and muscle development." Journal of Endocrinology 165, no. 2 (May 1, 2000): 457–66. http://dx.doi.org/10.1677/joe.0.1650457.

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We previously isolated a mammalian gene STC1 that encodes a glycoprotein related to stanniocalcin (STC), a fish hormone that plays a major role in calcium homeostasis. However, the mammalian STC1 gene is expressed in a variety of adult tissues in contrast to fish where STC is expressed only in one unique gland, the corpuscles of Stannius. This suggested that STC1 may have wider autocrine/paracrine functions in mammals. In the present study, using immunocytochemistry, we showed that STC1 protein is localized in the developing bone and muscle of the mouse fetus. During endochondral bone formatio

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Chang, Chi-Lun, Yu-Ju Chen, Carlo Giovanni Quintanilla, Ting-Sung Hsieh, and Jen Liou. "EB1 binding restricts STIM1 translocation to ER–PM junctions and regulates store-operated Ca2+ entry." Journal of Cell Biology 217, no. 6 (March 21, 2018): 2047–58. http://dx.doi.org/10.1083/jcb.201711151.

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The endoplasmic reticulum (ER) Ca2+ sensor STIM1 forms oligomers and translocates to ER–plasma membrane (PM) junctions to activate store-operated Ca2+ entry (SOCE) after ER Ca2+ depletion. STIM1 also interacts with EB1 and dynamically tracks microtubule (MT) plus ends. Nevertheless, the role of STIM1–EB1 interaction in regulating SOCE remains unresolved. Using live-cell imaging combined with a synthetic construct approach, we found that EB1 binding constitutes a trapping mechanism restricting STIM1 targeting to ER–PM junctions. We further showed that STIM1 oligomers retain EB1 binding ability

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Pascual-Caro, Carlos, Yolanda Orantos-Aguilera, Irene Sanchez-Lopez, Jaime de Juan-Sanz, Jan B. Parys, Estela Area-Gomez, Eulalia Pozo-Guisado, and Francisco Javier Martin-Romero. "STIM1 Deficiency Leads to Specific Down-Regulation of ITPR3 in SH-SY5Y Cells." International Journal of Molecular Sciences 21, no. 18 (September 9, 2020): 6598. http://dx.doi.org/10.3390/ijms21186598.

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STIM1 is an endoplasmic reticulum (ER) protein that modulates the activity of a number of Ca2+ transport systems. By direct physical interaction with ORAI1, a plasma membrane Ca2+ channel, STIM1 activates the ICRAC current, whereas the binding with the voltage-operated Ca2+ channel CaV1.2 inhibits the current through this latter channel. In this way, STIM1 is a key regulator of Ca2+ signaling in excitable and non-excitable cells, and altered STIM1 levels have been reported to underlie several pathologies, including immunodeficiency, neurodegenerative diseases, and cancer. In both sporadic and

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Chang, Andy C. M., Jeon Cha, Frank Koentgen, and Roger R. Reddel. "The Murine Stanniocalcin 1 Gene Is Not Essential for Growth and Development." Molecular and Cellular Biology 25, no. 23 (December 1, 2005): 10604–10. http://dx.doi.org/10.1128/mcb.25.23.10604-10610.2005.

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ABSTRACT The stanniocalcin 1 (STC1) gene is expressed in a wide variety of tissues, including the kidney, prostate, thyroid, bone, and ovary. STC1 protein is considered to have roles in many physiological processes, including bone development, reproduction, wound healing, angiogenesis, and modulation of inflammatory response. In fish, STC1 is a hormone that is secreted by the corpuscles of Stannius and is involved in calcium and phosphate homeostasis. To determine the role of STC1 in mammals, we generated Stc1-null mice by gene targeting. The number of Stc1 − / − mice obtained was in accordanc

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Laurent, B. C., X. Yang, and M. Carlson. "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family." Molecular and Cellular Biology 12, no. 4 (April 1992): 1893–902. http://dx.doi.org/10.1128/mcb.12.4.1893.

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The Saccharomyces cerevisiae SNF2 gene affects the expression of many diversely regulated genes and has been implicated in transcriptional activation. We report here the cloning and characterization of STH1, a gene that is homologous to SNF2. STH1 is essential for mitotic growth and is functionally distinct from SNF2. A bifunctional STH1-beta-galactosidase protein is located in the nucleus. The predicted 155,914-Da STH1 protein is 72% identical to SNF2 over 661 amino acids and 46% identical over another stretch of 66 amino acids. Both STH1 and SNF2 contain a putative nucleoside triphosphate-bi

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Laurent, B. C., X. Yang, and M. Carlson. "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family." Molecular and Cellular Biology 12, no. 4 (April 1992): 1893–902. http://dx.doi.org/10.1128/mcb.12.4.1893-1902.1992.

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The Saccharomyces cerevisiae SNF2 gene affects the expression of many diversely regulated genes and has been implicated in transcriptional activation. We report here the cloning and characterization of STH1, a gene that is homologous to SNF2. STH1 is essential for mitotic growth and is functionally distinct from SNF2. A bifunctional STH1-beta-galactosidase protein is located in the nucleus. The predicted 155,914-Da STH1 protein is 72% identical to SNF2 over 661 amino acids and 46% identical over another stretch of 66 amino acids. Both STH1 and SNF2 contain a putative nucleoside triphosphate-bi

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Albarrán, Letizia, José J. López, Luis J. Gómez, Ginés M. Salido, and Juan A. Rosado. "SARAF modulates TRPC1, but not TRPC6, channel function in a STIM1-independent manner." Biochemical Journal 473, no. 20 (October 11, 2016): 3581–95. http://dx.doi.org/10.1042/bcj20160348.

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Canonical transient receptor potential-1 (TRPC1) is an almost ubiquitously expressed channel that plays a relevant role in cell function. As other TRPC members, TRPC1 forms receptor-operated cation channels that exhibit both STIM1-dependent and store-independent behaviour. The STIM1 inhibitor SARAF (for store-operated Ca2+ entry (SOCE)-associated regulatory factor) modulates SOCE by interaction with the STIM1 region responsible for Orai1 activation (SOAR). Furthermore, SARAF modulates Ca2+ entry through the arachidonate-regulated Ca2+ (ARC) channels, consisting of Orai1 and Orai3 heteropentame

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Lee, Keon Jin, Jin Seok Woo, Ji-Hye Hwang, Changdo Hyun, Chung-Hyun Cho, Do Han Kim, and Eun Hui Lee. "STIM1 negatively regulates Ca2+ release from the sarcoplasmic reticulum in skeletal myotubes." Biochemical Journal 453, no. 2 (June 28, 2013): 187–200. http://dx.doi.org/10.1042/bj20130178.

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STIM1 (stromal interaction molecule 1) mediates SOCE (store-operated Ca2+ entry) in skeletal muscle. However, the direct role(s) of STIM1 in skeletal muscle, such as Ca2+ release from the SR (sarcoplasmic reticulum) for muscle contraction, have not been identified. The times required for the maximal expression of endogenous STIM1 or Orai1, or for the appearance of puncta during the differentiation of mouse primary skeletal myoblasts to myotubes, were all different, and the formation of puncta was detected with no stimulus during differentiation, suggesting that, in skeletal muscle, the formati

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Wang, Yanxia, Sarika Chaudhari, Yuezhong Ren та Rong Ma. "Impairment of hepatic nuclear factor-4α binding to the Stim1 promoter contributes to high glucose-induced upregulation of STIM1 expression in glomerular mesangial cells". American Journal of Physiology-Renal Physiology 308, № 10 (15 травня 2015): F1135—F1145. http://dx.doi.org/10.1152/ajprenal.00563.2014.

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The present study was carried out to investigate if hepatic nuclear factor (HNF)4α contributed to the high glucose-induced increase in stromal interacting molecule (STIM)1 protein abundance in glomerular mesangial cells (MCs). Western blot and immunofluorescence experiments showed HNF4α expression in MCs. Knockdown of HNF4α using a small interfering RNA approach significantly increased mRNA expression levels of both STIM1 and Orai1 and protein expression levels of STIM1 in cultured human MCs. Consistently, overexpression of HNF4α reduced expressed STIM1 protein expression in human embryonic ki

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Chang, H. C., D. F. Nathan, and S. Lindquist. "In vivo analysis of the Hsp90 cochaperone Sti1 (p60)." Molecular and Cellular Biology 17, no. 1 (January 1997): 318–25. http://dx.doi.org/10.1128/mcb.17.1.318.

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Hsp90 interacts with Sti1 (p60) in lysates of yeast and vertebrate cells. Here we provide the first analysis of their interaction in vivo. Saccharomyces cerevisiae mutations that eliminate Sti1 or reduce intracellular concentrations of Hsp90 individually have little or no effect on growth at normal temperatures. However, when combined, the mutations greatly reduce or eliminate growth. Furthermore, overexpression of Sti1 has allele-specific effects on cells carrying various hsp90ts point mutations. These genetic interactions provide strong evidence that Hsp90 and Sti1 interact in vivo and that

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