scholarly journals Association of the Yeast RNA-binding Protein She2p with the Tubular Endoplasmic Reticulum Depends on Membrane Curvature

2013 ◽  
Vol 288 (45) ◽  
pp. 32384-32393 ◽  
Author(s):  
Christian Genz ◽  
Julia Fundakowski ◽  
Orit Hermesh ◽  
Maria Schmid ◽  
Ralf-Peter Jansen
RNA ◽  
2018 ◽  
Vol 24 (5) ◽  
pp. 688-703 ◽  
Author(s):  
Jack C.-C. Hsu ◽  
David W. Reid ◽  
Alyson M. Hoffman ◽  
Devanand Sarkar ◽  
Christopher V. Nicchitta

2019 ◽  
Vol 179 (3) ◽  
pp. 1111-1131 ◽  
Author(s):  
Li Tian ◽  
Hong-Li Chou ◽  
Laining Zhang ◽  
Thomas W. Okita

1999 ◽  
Vol 19 (3) ◽  
pp. 2220-2230 ◽  
Author(s):  
Louise Wickham ◽  
Thomas Duchaîne ◽  
Ming Luo ◽  
Ivan R. Nabi ◽  
Luc DesGroseillers

ABSTRACT Staufen (Stau) is a double-stranded RNA (dsRNA)-binding protein involved in mRNA transport and localization in Drosophila.To understand the molecular mechanisms of mRNA transport in mammals, we cloned human (hStau) and mouse (mStau)staufen cDNAs. In humans, four transcripts arise by differential splicing of the Stau gene and code for two proteins with different N-terminal extremities. In vitro, hStau and mStau bind dsRNA via each of two full-length dsRNA-binding domains and tubulin via a region similar to the microtubule-binding domain of MAP-1B, suggesting that Stau cross-links cytoskeletal and RNA components. Immunofluorescent double labeling of transfected mammalian cells revealed that Stau is localized to the rough endoplasmic reticulum (RER), implicating this RNA-binding protein in mRNA targeting to the RER, perhaps via a multistep process involving microtubules. These results are the first demonstration of the association of an RNA-binding protein in addition to ribosomal proteins, with the RER, implicating this class of proteins in the transport of RNA to its site of translation.


2021 ◽  
Author(s):  
Fatima Cairrao ◽  
Cristiana C Santos ◽  
Adrien Le Thomas ◽  
Scot Marsters ◽  
Avi Ashkenazi ◽  
...  

SUMMARYThe unfolded protein response (UPR) maintains homeostasis of the endoplasmic reticulum(ER). Residing in the ER membrane, the UPR mediator Ire1 deploys its cytoplasmic kinase-endoribonuclease domain to activate the key UPR transcription factor Xbp1 through non-conventional splicing of Xbp1 mRNA. Ire1 also degrades diverse ER-targeted mRNAs through regulated Ire1-dependent decay (RIDD), but how it spares Xbp1 mRNA from this decay is unknown. We identified binding sites for the RNA-binding protein Pumilio in the 3’UTR Drosophila Xbp1. In the developing Drosophila eye, Pumilio bound both the Xbp1unspliced and Xbp1spliced mRNAs, but only Xbp1spliced was stabilized by Pumilio. Furthermore, Pumilio displayed Ire1 kinase-dependent phosphorylation during ER stress, which was required for its stabilization of Xbp1spliced. Human IRE1 could directly phosphorylate Pumilio, and phosphorylated Pumilio protected Xbp1spliced mRNA against RIDD. Thus, Ire1-mediated phosphorylation enables Pumilio to shield Xbp1spliced from RIDD. These results uncover an important and unexpected regulatory link between an RNA-binding protein and the UPR.


2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  

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