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Journal articles on the topic 'Staufen2'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Almasi, Shekoufeh, and Bernard J. Jasmin. "The multifunctional RNA-binding protein Staufen1: an emerging regulator of oncogenesis through its various roles in key cellular events." Cellular and Molecular Life Sciences 78, no. 23 (2021): 7145–60. http://dx.doi.org/10.1007/s00018-021-03965-w.

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AbstractThe double-stranded multifunctional RNA-binding protein (dsRBP) Staufen was initially discovered in insects as a regulator of mRNA localization. Later, its mammalian orthologs have been described in different organisms, including humans. Two human orthologues of Staufen, named Staufen1 (STAU1) and Staufen2 (STAU2), share some structural and functional similarities. However, given their different spatio-temporal expression patterns, each of these orthologues plays distinct roles in cells. In the current review, we focus on the role of STAU1 in cell functions and cancer development. Sinc

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2

Duchaîne, Thomas F., Indradeo Hemraj, Luc Furic, Anke Deitinghoff, Michael A. Kiebler, and Luc DesGroseillers. "Staufen2 isoforms localize to the somatodendritic domain of neurons and interact with different organelles." Journal of Cell Science 115, no. 16 (2002): 3285–95. http://dx.doi.org/10.1242/jcs.115.16.3285.

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Mammalian Staufen2 (Stau2) is involved in mRNA transport in neurons. Here,we report that Stau2 is a double-stranded RNA-binding protein that is mainly expressed in the brain. We show that Stau2 is found in the somatodendritic compartment of neurons. In dendrites, Stau2 is aligned on individual tracts and colocalizes with microtubules. Stau2 is expressed as at least three splice isoforms, which can be observed in several subcellular complexes. Although a 62 kDa isoform (Stau262) fractionates in ribosome-free fractions of light density, Stau259 and Stau252 are found in high-density complexes. Th

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3

Bélanger, Guy, Mark A. Stocksley, Marie Vandromme, et al. "Localization of the RNA-binding proteins Staufen1 and Staufen2 at the mammalian neuromuscular junction." Journal of Neurochemistry 86, no. 3 (2003): 669–77. http://dx.doi.org/10.1046/j.1471-4159.2003.01883.x.

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4

Heraud-Farlow, Jacki E., Tejaswini Sharangdhar, Xiao Li, et al. "Staufen2 Regulates Neuronal Target RNAs." Cell Reports 5, no. 6 (2013): 1511–18. http://dx.doi.org/10.1016/j.celrep.2013.11.039.

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5

Fernández-Moya, Sandra M., Janina Ehses, Karl E. Bauer, et al. "RGS4 RNA Secondary Structure Mediates Staufen2 RNP Assembly in Neurons." International Journal of Molecular Sciences 22, no. 23 (2021): 13021. http://dx.doi.org/10.3390/ijms222313021.

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RNA-binding proteins (RBPs) act as posttranscriptional regulators controlling the fate of target mRNAs. Unraveling how RNAs are recognized by RBPs and in turn are assembled into neuronal RNA granules is therefore key to understanding the underlying mechanism. While RNA sequence elements have been extensively characterized, the functional impact of RNA secondary structures is only recently being explored. Here, we show that Staufen2 binds complex, long-ranged RNA hairpins in the 3′-untranslated region (UTR) of its targets. These structures are involved in the assembly of Staufen2 into RNA granu

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6

Ramasamy, Srinivas, Hui Wang, Helen Ngoc Bao Quach, and Karuna Sampath. "Zebrafish Staufen1 and Staufen2 are required for the survival and migration of primordial germ cells." Developmental Biology 292, no. 2 (2006): 393–406. http://dx.doi.org/10.1016/j.ydbio.2006.01.014.

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7

Schieweck, Rico, Therese Riedemann, Ignasi Forné, et al. "Pumilio2 and Staufen2 selectively balance the synaptic proteome." Cell Reports 35, no. 12 (2021): 109279. http://dx.doi.org/10.1016/j.celrep.2021.109279.

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8

Macchi, Paolo, Amy M. Brownawell, Barbara Grunewald, Luc DesGroseillers, Ian G. Macara, and Michael A. Kiebler. "The Brain-specific Double-stranded RNA-binding Protein Staufen2." Journal of Biological Chemistry 279, no. 30 (2004): 31440–44. http://dx.doi.org/10.1074/jbc.c400226200.

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9

Bilogan, Cassandra K., and Marko E. Horb. "Xenopus staufen2 is required for anterior endodermal organ formation." genesis 50, no. 3 (2012): 251–59. http://dx.doi.org/10.1002/dvg.22000.

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10

Furic, L., M. Maher-Laporte, and L. DesGroseillers. "A genome-wide approach identifies distinct but overlapping subsets of cellular mRNAs associated with Staufen1- and Staufen2-containing ribonucleoprotein complexes." RNA 14, no. 2 (2007): 324–35. http://dx.doi.org/10.1261/rna.720308.

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11

Maher-Laporte, Marjolaine, Frédéric Berthiaume, Mireille Moreau, et al. "Molecular Composition of Staufen2-Containing Ribonucleoproteins in Embryonic Rat Brain." PLoS ONE 5, no. 6 (2010): e11350. http://dx.doi.org/10.1371/journal.pone.0011350.

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12

Popper, Bastian, Antonia Demleitner, Valerie J. Bolivar, et al. "Staufen2 deficiency leads to impaired response to novelty in mice." Neurobiology of Learning and Memory 150 (April 2018): 107–15. http://dx.doi.org/10.1016/j.nlm.2018.02.027.

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13

Park, E., M. L. Gleghorn, and L. E. Maquat. "Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity." Proceedings of the National Academy of Sciences 110, no. 2 (2012): 405–12. http://dx.doi.org/10.1073/pnas.1213508110.

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14

Maher-Laporte, Marjolaine, and Luc DesGroseillers. "Genome wide identification of Staufen2-bound mRNAs in embryonic rat brains." BMB Reports 43, no. 5 (2010): 344–48. http://dx.doi.org/10.5483/bmbrep.2010.43.5.344.

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15

Miki, Takashi, Yasunao Kamikawa, Sadamu Kurono, Yuka Kaneko, Jun Katahira, and Yoshihiro Yoneda. "Cell type-dependent gene regulation by Staufen2 in conjunction with Upf1." BMC Molecular Biology 12, no. 1 (2011): 48. http://dx.doi.org/10.1186/1471-2199-12-48.

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16

Ravel-Chapuis, Aymeric, Tara E. Crawford, Marie-Laure Blais-Crépeau, Guy Bélanger, Chase T. Richer, and Bernard J. Jasmin. "The RNA-binding protein Staufen1 impairs myogenic differentiation via a c-myc–dependent mechanism." Molecular Biology of the Cell 25, no. 23 (2014): 3765–78. http://dx.doi.org/10.1091/mbc.e14-04-0895.

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Recent work has shown that Staufen1 plays key roles in skeletal muscle, yet little is known about its pattern of expression during embryonic and postnatal development. Here we first show that Staufen1 levels are abundant in mouse embryonic muscles and that its expression decreases thereafter, reaching low levels in mature muscles. A similar pattern of expression is seen as cultured myoblasts differentiate into myotubes. Muscle degeneration/regeneration experiments revealed that Staufen1 increases after cardiotoxin injection before returning to the low levels seen in mature muscles. We next pre

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17

Ortiz, Raúl, Maya V. Georgieva, Sara Gutiérrez, Neus Pedraza, Sandra M. Fernández-Moya та Carme Gallego. "Recruitment of Staufen2 Enhances Dendritic Localization of an Intron-Containing CaMKIIα mRNA". Cell Reports 20, № 1 (2017): 13–20. http://dx.doi.org/10.1016/j.celrep.2017.06.026.

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18

Lazzaretti, Daniela, Lina Bandholz-Cajamarca, Christiane Emmerich, et al. "The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity." Life Science Alliance 1, no. 5 (2018): e201800187. http://dx.doi.org/10.26508/lsa.201800187.

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During mRNA localization, RNA-binding proteins interact with specific structured mRNA localization motifs. Although several such motifs have been identified, we have limited structural information on how these interact with RNA-binding proteins. Staufen proteins bind structured mRNA motifs through dsRNA-binding domains (dsRBD) and are involved in mRNA localization in Drosophila and mammals. We solved the structure of two dsRBDs of human Staufen1 in complex with a physiological dsRNA sequence. We identified interactions between the dsRBDs and the RNA sugar–phosphate backbone and direct contacts

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19

Miki, Takashi, and Yoshihiro Yoneda. "Alternative Splicing of Staufen2 Creates the Nuclear Export Signal for CRM1 (Exportin 1)." Journal of Biological Chemistry 279, no. 46 (2004): 47473–79. http://dx.doi.org/10.1074/jbc.m407883200.

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20

Vessey, John P., Gianluca Amadei, Sarah E. Burns, Michael A. Kiebler, David R. Kaplan, and Freda D. Miller. "An Asymmetrically Localized Staufen2-Dependent RNA Complex Regulates Maintenance of Mammalian Neural Stem Cells." Cell Stem Cell 11, no. 4 (2012): 517–28. http://dx.doi.org/10.1016/j.stem.2012.06.010.

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21

Berger, Stefan M., Iván Fernández-Lamo, Kai Schönig, et al. "Forebrain-specific, conditional silencing of Staufen2 alters synaptic plasticity, learning, and memory in rats." Genome Biology 18, no. 1 (2017): 222. https://doi.org/10.1186/s13059-017-1350-8.

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<strong>Background: </strong>Dendritic messenger RNA (mRNA) localization and subsequent local translation in dendrites critically contributes to synaptic plasticity and learning and memory. Little is known, however, about the contribution of RNA-binding proteins (RBPs) to these processes in vivo.<strong>Results: </strong>To delineate the role of the double-stranded RBP Staufen2 (Stau2), we generate a transgenic rat model, in which Stau2 expression is conditionally silenced by Cre-inducible expression of a microRNA (miRNA) targeting Stau2 mRNA in adult forebrain neurons. Known physiological mRN

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22

Pernice, Helena F., Rico Schieweck, Mehrnoosh Jafari, et al. "Altered Glutamate Receptor Ionotropic Delta Subunit 2 Expression in Stau2-Deficient Cerebellar Purkinje Cells in the Adult Brain." International Journal of Molecular Sciences 20, no. 7 (2019): 1797. http://dx.doi.org/10.3390/ijms20071797.

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Staufen2 (Stau2) is an RNA-binding protein that is involved in dendritic spine morphogenesis and function. Several studies have recently investigated the role of Stau2 in the regulation of its neuronal target mRNAs, with particular focus on the hippocampus. Here, we provide evidence for Stau2 expression and function in cerebellar Purkinje cells. We show that Stau2 downregulation (Stau2GT) led to an increase of glutamate receptor ionotropic delta subunit 2 (GluD2) in Purkinje cells when animals performed physical activity by voluntary wheel running compared with the age-matched wildtype (WT) mi

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23

Chatel-Chaix, Laurent, Jean-Francois Clément, Catherine Martel, et al. "Identification of Staufen in the Human Immunodeficiency Virus Type 1 Gag Ribonucleoprotein Complex and a Role in Generating Infectious Viral Particles." Molecular and Cellular Biology 24, no. 7 (2004): 2637–48. http://dx.doi.org/10.1128/mcb.24.7.2637-2648.2004.

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ABSTRACT Staufen is a host protein that is selectively incorporated into human immunodeficiency virus type 1 (HIV-1) particles in a poorly defined process that involves the selection of HIV-1 genomic RNA for encapsidation and the activity of its third double-stranded RNA-binding domain (dsRBD3). To better understand this, we characterized its interactions with pr55Gag, the principal mediator of HIV-1 genomic RNA encapsidation. Chimeric proviruses harboring wild-type or mutant forms of Staufen were expressed in 293T cells. Cell fractionation analyses demonstrated that Staufen cosedimented with

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24

Zhang, Xin, Véronique Trépanier, Remy Beaujois, Wildriss Viranaicken, Elliot Drobetsky, and Luc DesGroseillers. "The downregulation of the RNA-binding protein Staufen2 in response to DNA damage promotes apoptosis." Nucleic Acids Research 44, no. 8 (2016): 3695–712. http://dx.doi.org/10.1093/nar/gkw057.

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25

Monshausen, Michaela, Niels H. Gehring, and Kenneth S. Kosik. "The Mammalian RNA-Binding Protein Staufen2 Links Nuclear and Cytoplasmic RNA Processing Pathways in Neurons." NeuroMolecular Medicine 6, no. 2-3 (2004): 127–44. http://dx.doi.org/10.1385/nmm:6:2-3:127.

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26

Goetze, Bernhard, Fabian Tuebing, Yunli Xie, et al. "The brain-specific double-stranded RNA-binding protein Staufen2 is required for dendritic spine morphogenesis." Journal of Cell Biology 172, no. 2 (2006): 221–31. http://dx.doi.org/10.1083/jcb.200509035.

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Mammalian Staufen2 (Stau2) is a member of the double-stranded RNA-binding protein family. Its expression is largely restricted to the brain. It is thought to play a role in the delivery of RNA to dendrites of polarized neurons. To investigate the function of Stau2 in mature neurons, we interfered with Stau2 expression by RNA interference (RNAi). Mature neurons lacking Stau2 displayed a significant reduction in the number of dendritic spines and an increase in filopodia-like structures. The number of PSD95-positive synapses and miniature excitatory postsynaptic currents were markedly reduced in

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27

Nam, Yeon-Ju, Hyo-Soon Cheon, Young-Ki Choi, et al. "Role of mitogen-activated protein kinase (MAPK) docking sites on Staufen2 protein in dendritic mRNA transport." Biochemical and Biophysical Research Communications 372, no. 4 (2008): 525–29. http://dx.doi.org/10.1016/j.bbrc.2008.05.047.

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28

Lucas, Bronwyn A., Eitan Lavi, Lily Shiue, et al. "Evidence for convergent evolution of SINE-directed Staufen-mediated mRNA decay." Proceedings of the National Academy of Sciences 115, no. 5 (2018): 968–73. http://dx.doi.org/10.1073/pnas.1715531115.

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Primate-specific Alu short interspersed elements (SINEs) as well as rodent-specific B and ID (B/ID) SINEs can promote Staufen-mediated decay (SMD) when present in mRNA 3′-untranslated regions (3′-UTRs). The transposable nature of SINEs, their presence in long noncoding RNAs, their interactions with Staufen, and their rapid divergence in different evolutionary lineages suggest they could have generated substantial modification of posttranscriptional gene-control networks during mammalian evolution. Some of the variation in SMD regulation produced by SINE insertion might have had a similar regul

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29

Kusek, Gretchen, Melissa Campbell, Frank Doyle, Scott A. Tenenbaum, Michael Kiebler, and Sally Temple. "Asymmetric Segregation of the Double-Stranded RNA Binding Protein Staufen2 during Mammalian Neural Stem Cell Divisions Promotes Lineage Progression." Cell Stem Cell 11, no. 4 (2012): 505–16. http://dx.doi.org/10.1016/j.stem.2012.06.006.

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30

Zheng, Yun-Xiao, Lei Wang, Wei-Sha Kong, et al. "Nsp2 has the potential to be a drug target revealed by global identification of SARS-CoV-2 Nsp2-interacting proteins." Acta Biochimica et Biophysica Sinica 53, no. 9 (2021): 1134–41. http://dx.doi.org/10.1093/abbs/gmab088.

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Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has become a global health threat since December 2019, and there is still no highly effective drug to control the pandemic. To facilitate drug target identification for drug development, studies on molecular mechanisms, such as SARS-CoV-2 protein interactions, are urgently needed. In this study, we focused on Nsp2, a non-structural protein with largely unknown function and mechanism. The interactome of Nsp2 was revealed through the combination of affinity purification mass spectrometry (AP-MS) and stable isotope labeling by

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31

Li, Ying, Yeou-cherng Bor, Mark P. Fitzgerald, Kevin S. Lee, David Rekosh, and Marie-Louise Hammarskjold. "AnNXF1mRNA with a retained intron is expressed in hippocampal and neocortical neurons and is translated into a protein that functions as an Nxf1 cofactor." Molecular Biology of the Cell 27, no. 24 (2016): 3903–12. http://dx.doi.org/10.1091/mbc.e16-07-0515.

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The Nxf1 protein is a major nuclear export receptor for the transport of mRNA, and it also is essential for export of retroviral mRNAs with retained introns. In the latter case, it binds to RNA elements known as constitutive transport elements (CTEs) and functions in conjunction with a cofactor known as Nxt1. The NXF1 gene also regulates expression of its own intron-containing RNA through the use of a functional CTE within intron 10. mRNA containing this intron is exported to the cytoplasm, where it can be translated into the 356–amino acid short Nxf1(sNxf1) protein, despite the fact that it i

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32

Sharangdhar, Tejaswini, Yoichiro Sugimoto, Jacqueline Heraud‐Farlow, et al. "A retained intron in the 3′‐ UTR of Calm3 mRNA mediates its Staufen2‐ and activity‐dependent localization to neuronal dendrites." EMBO reports 18, no. 10 (2017): 1762–74. http://dx.doi.org/10.15252/embr.201744334.

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33

Bajaj, Jeevisha, Michael Hamilton, Yutaka Shima, et al. "An in vivo genome-wide CRISPR screen identifies the RNA-binding protein Staufen2 as a key regulator of myeloid leukemia." Nature Cancer 1, no. 4 (2020): 410–22. http://dx.doi.org/10.1038/s43018-020-0054-2.

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34

Jeong, Ji-Hye, Yeon-Ju Nam, Seok-Yong Kim, Eung-Gook Kim, Jooyoung Jeong, and Hyong Kyu Kim. "The transport of Staufen2-containing ribonucleoprotein complexes involves kinesin motor protein and is modulated by mitogen-activated protein kinase pathway." Journal of Neurochemistry 102, no. 6 (2007): 2073–84. http://dx.doi.org/10.1111/j.1471-4159.2007.04697.x.

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35

Thomas, María G., Leandro J. Martinez Tosar, Mariela Loschi, et al. "Staufen Recruitment into Stress Granules Does Not Affect Early mRNA Transport in Oligodendrocytes." Molecular Biology of the Cell 16, no. 1 (2005): 405–20. http://dx.doi.org/10.1091/mbc.e04-06-0516.

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Staufen is a conserved double-stranded RNA-binding protein required for mRNA localization in Drosophila oocytes and embryos. The mammalian homologues Staufen 1 and Staufen 2 have been implicated in dendritic RNA targeting in neurons. Here we show that in rodent oligodendrocytes, these two proteins are present in two independent sets of RNA granules located at the distal myelinating processes. A third kind of RNA granules lacks Staufen and contains major myelin mRNAs. Myelin Staufen granules associate with microfilaments and microtubules, and their subcellular distribution is affected by polyso

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36

Balakrishnan, Kannan, Ananda Jaguva Vasudevan, Krishnaveni Mohareer, Tom Luedde, Carsten Münk, and Sharmistha Banerjee. "Encapsidation of Staufen-2 Enhances Infectivity of HIV-1." Viruses 13, no. 12 (2021): 2459. http://dx.doi.org/10.3390/v13122459.

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Staufen, the RNA-binding family of proteins, affects various steps in the Human Immuno-Deficiency Virus (HIV-1) replication cycle. While our previous study established Staufen-2–HIV-1 Rev interaction and its role in augmenting nucleocytoplasmic export of RRE-containing viral RNA, viral incorporation of Staufen-2 and its effect on viral propagation were unknown. Here, we report that Staufen-2 interacts with HIV-1 Gag and is incorporated into virions and that encapsidated Staufen-2 boosted viral infectivity. Further, Staufen-2 gets co-packaged into virions, possibly by interacting with host fact

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37

Ramos, Hade, Anne Monette, Meijuan Niu, et al. "The double-stranded RNA-binding protein, Staufen1, is an IRES-transacting factor regulating HIV-1 cap-independent translation initiation." Nucleic Acids Research 50, no. 1 (2021): 411–29. http://dx.doi.org/10.1093/nar/gkab1188.

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Abstract Translation initiation of the viral genomic mRNA (vRNA) of human immunodeficiency virus-type 1 (HIV-1) can be mediated by a cap- or an internal ribosome entry site (IRES)-dependent mechanism. A previous report shows that Staufen1, a cellular double-stranded (ds) RNA-binding protein (RBP), binds to the 5’untranslated region (5′UTR) of the HIV-1 vRNA and promotes its cap-dependent translation. In this study, we now evaluate the role of Staufen1 as an HIV-1 IRES-transacting factor (ITAF). We first confirm that Staufen1 associates with both the HIV-1 vRNA and the Gag protein during HIV-1

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38

Blackham, Samantha L., and Michael J. McGarvey. "A host cell RNA-binding protein, Staufen1, has a role in hepatitis C virus replication before virus assembly." Journal of General Virology 94, no. 11 (2013): 2429–36. http://dx.doi.org/10.1099/vir.0.051383-0.

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Staufen1 is a dsRNA-binding protein involved in the regulation of translation and the trafficking and degradation of cellular RNAs. Staufen1 has also been shown to stimulate translation of human immunodeficiency virus type 1 (HIV-1) RNA, regulate HIV-1 and influenza A virus assembly, and there is also indication that it can interact with hepatitis C virus (HCV) RNA. To investigate the role of Staufen1 in the HCV replication cycle, the effects of small interfering RNA knockout of Staufen1 on HCV strain JFH-1 replication and the intracellular distribution of the Staufen1 protein during HCV infec

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Ravel-Chapuis, Aymeric, Guy Bélanger, Ramesh S. Yadava, et al. "The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing." Journal of Cell Biology 196, no. 6 (2012): 699–712. http://dx.doi.org/10.1083/jcb.201108113.

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In myotonic dystrophy type 1 (DM1), dystrophia myotonica protein kinase messenger ribonucleic acids (RNAs; mRNAs) with expanded CUG repeats (CUGexp) aggregate in the nucleus and become toxic to cells by sequestering and/or misregulating RNA-binding proteins, resulting in aberrant alternative splicing. In this paper, we find that the RNA-binding protein Staufen1 is markedly and specifically increased in skeletal muscle from DM1 mouse models and patients. We show that Staufen1 interacts with mutant CUGexp mRNAs and promotes their nuclear export and translation. This effect is critically dependen

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40

Crawford Parks, Tara E., Kristen A. Marcellus, Christine Péladeau, Bernard J. Jasmin, and Aymeric Ravel-Chapuis. "Overexpression of Staufen1 in DM1 mouse skeletal muscle exacerbates dystrophic and atrophic features." Human Molecular Genetics 29, no. 13 (2020): 2185–99. http://dx.doi.org/10.1093/hmg/ddaa111.

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Abstract In myotonic dystrophy type 1 (DM1), the CUG expansion (CUGexp) in the 3′ untranslated region of the dystrophia myotonica protein kinase messenger ribonucleic acid affects the homeostasis of ribonucleic acid-binding proteins, causing the multiple symptoms of DM1. We have previously reported that Staufen1 is increased in skeletal muscles from DM1 mice and patients and that sustained Staufen1 expression in mature mouse muscle causes a progressive myopathy. Here, we hypothesized that the elevated levels of Staufen1 contributes to the myopathic features of the disease. Interestingly, the c

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41

Hurst, S., N. J. Talbot, and H. Stebbings. "A staufen-like RNA-binding protein in translocation channels linking nurse cells to oocytes in Notonecta shows nucleotide-dependent attachment to microtubules." Journal of Cell Science 112, no. 17 (1999): 2947–55. http://dx.doi.org/10.1242/jcs.112.17.2947.

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In Drosophila melanogaster the staufen gene encodes an RNA-binding protein that is essential for the correct localization of certain nurse cell-derived transcripts in oocytes. Although the mechanism underlying mRNA localization is unknown, mRNA-staufen complexes have been shown to move in a microtubule-dependent manner, and it has been suggested that staufen associates with a motor protein which generates the movement. We have investigated this possibility using Notonecta glauca in which nurse cells also supply the oocytes with mRNA, but via greatly extended nutritive tubes comprised of large

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42

BRENDEL, Cornelia, Monika REHBEIN, Hans-Jürgen KREIENKAMP, Friedrich BUCK, Dietmar RICHTER, and Stefan KINDLER. "Characterization of Staufen 1 ribonucleoprotein complexes." Biochemical Journal 384, no. 2 (2004): 239–46. http://dx.doi.org/10.1042/bj20040812.

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In Drosophila oocytes and neuroblasts, the double-stranded RNA binding protein Staufen assembles into ribonucleoprotein particles, which mediate cytoplasmic mRNA trafficking and translation. Two different mammalian orthologues also appear to reside in distinct RNA-containing particles. To date, relatively little is known about the molecular composition of Staufen-containing ribonucleoprotein complexes. Here, we have used a novel one-step affinity purification protocol to identify components of Staufen 1-containing particles. Whereas the nucleocytoplasmic RNA-binding protein nucleolin is linked

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43

Kim, Eun Seon, Chang Geon Chung, Jeong Hyang Park, et al. "C9orf72-associated arginine-rich dipeptide repeats induce RNA-dependent nuclear accumulation of Staufen in neurons." Human Molecular Genetics 30, no. 12 (2021): 1084–100. http://dx.doi.org/10.1093/hmg/ddab089.

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Abstract RNA-binding proteins (RBPs) play essential roles in diverse cellular processes through post-transcriptional regulation of RNAs. The subcellular localization of RBPs is thus under tight control, the breakdown of which is associated with aberrant cytoplasmic accumulation of nuclear RBPs such as TDP-43 and FUS, well-known pathological markers for amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). Here, we report in Drosophila model for ALS/FTD that nuclear accumulation of a cytoplasmic RBP Staufen may be a new pathological feature. We found that in Drosophila C4da neuro

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Yoon, June-Sun, Kanakachari Mogilicherla, Dhandapani Gurusamy, Xien Chen, Shankar C. R. R. Chereddy, and Subba Reddy Palli. "Double-stranded RNA binding protein, Staufen, is required for the initiation of RNAi in coleopteran insects." Proceedings of the National Academy of Sciences 115, no. 33 (2018): 8334–39. http://dx.doi.org/10.1073/pnas.1809381115.

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RNA interference (RNAi) is being used to develop methods to control pests and disease vectors. RNAi is robust and systemic in coleopteran insects but is quite variable in other insects. The determinants of efficient RNAi in coleopterans, as well as its potential mechanisms of resistance, are not known. RNAi screen identified a double-stranded RNA binding protein (StaufenC) as a major player in RNAi. StaufenC homologs have been identified in only coleopteran insects. Experiments in two coleopteran insects, Leptinotarsa decemlineata and Tribolium castaneum, showed the requirement of StaufenC for

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Matsuzaki, F., T. Ohshiro, H. Ikeshima-Kataoka, and H. Izumi. "miranda localizes staufen and prospero asymmetrically in mitotic neuroblasts and epithelial cells in early Drosophila embryogenesis." Development 125, no. 20 (1998): 4089–98. http://dx.doi.org/10.1242/dev.125.20.4089.

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When neuroblasts divide, prospero protein and mRNA segregate asymmetrically into the daughter neuroblast and sibling ganglion mother cell. miranda is known to localize prospero protein to the basal cell cortex of neuroblasts while the staufen RNA-binding protein mediates prospero mRNA localization. Here we show that miranda is required for asymmetric staufen localization in neuroblasts. Analyses using miranda mutants reveal that prospero and staufen interact with miranda under the same cell-cycle-dependent control. miranda thus acts to partition both prospero protein and mRNA. Furthermore, mir

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Mohr, Sabine, Andrew Kenny, Simon T. Y. Lam, et al. "Opposing roles for Egalitarian and Staufen in transport, anchoring and localization of oskar mRNA in the Drosophila oocyte." PLOS Genetics 17, no. 4 (2021): e1009500. http://dx.doi.org/10.1371/journal.pgen.1009500.

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Localization ofoskarmRNA includes two distinct phases: transport from nurse cells to the oocyte, a process typically accompanied by cortical anchoring in the oocyte, followed by posterior localization within the oocyte. Signals within theoskar3’ UTR directing transport are individually weak, a feature previously hypothesized to facilitate exchange between the different localization machineries. We show that alteration of the SL2a stem-loop structure containing theoskartransport and anchoring signal (TAS) removes an inhibitory effect such thatin vitrobinding by the RNA transport factor, Egalita

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Köhrmann, Martin, Ming Luo, Christoph Kaether, Luc DesGroseillers, Carlos G. Dotti, and Michael A. Kiebler. "Microtubule-dependent Recruitment of Staufen-Green Fluorescent Protein into Large RNA-containing Granules and Subsequent Dendritic Transport in Living Hippocampal Neurons." Molecular Biology of the Cell 10, no. 9 (1999): 2945–53. http://dx.doi.org/10.1091/mbc.10.9.2945.

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Dendritic mRNA transport and local translation at individual potentiated synapses may represent an elegant way to form synaptic memory. Recently, we characterized Staufen, a double-stranded RNA-binding protein, in rat hippocampal neurons and showed its presence in large RNA-containing granules, which colocalize with microtubules in dendrites. In this paper, we transiently transfect hippocampal neurons with human Staufen-green fluorescent protein (GFP) and find fluorescent granules in the somatodendritic domain of these cells. Human Stau-GFP granules show the same cellular distribution and size

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Paul, Sharan, Warunee Dansithong, Karla P. Figueroa, Mandi Gandelman, Daniel R. Scoles, and Stefan M. Pulst. "Staufen1 in Human Neurodegeneration." Annals of Neurology 89, no. 6 (2021): 1114–28. http://dx.doi.org/10.1002/ana.26069.

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Meyer, Erika L., and Elizabeth R. Gavis. "Staufen does double duty." Nature Structural & Molecular Biology 12, no. 4 (2005): 291–92. http://dx.doi.org/10.1038/nsmb0405-291.

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Park, Eonyoung, and Lynne E. Maquat. "Staufen-mediated mRNA decay." Wiley Interdisciplinary Reviews: RNA 4, no. 4 (2013): 423–35. http://dx.doi.org/10.1002/wrna.1168.

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