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A direct interaction between the RNA-binding proteins Staufen and Tm1-I/C in the oskar mRNA transport complex

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00009101
URN to cite this document: urn:nbn:de:bvb:703-epub-9101-6

Title data

Gaber, Thomas ; Monecke, Thomas ; Grabowski, Julia ; Simon, Bernd ; Williams, Tobias ; Roman, Vera ; Chao, Jeffrey ; Hennig, Janosch ; Ephrussi, Anne ; Niessing, Dierk ; Heber, Simone:
A direct interaction between the RNA-binding proteins Staufen and Tm1-I/C in the oskar mRNA transport complex.
In: Cell Reports. Vol. 44 (2025) Issue 7 . - 115906.
ISSN 2211-1247
DOI der Verlagsversion: https://doi.org/10.1016/j.celrep.2025.115906

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Project information

Project title:
Project's official title
Project's id
FOR 2333: Makromolekulare Komplexe in der mRNA Lokalisation
270067186
SPP 1935: Deciphering the mRNP code: RNA-bound determinants of post-transcriptional gene regulation
273941853
Open Access Publizieren
No information

Project financing: Deutsche Forschungsgemeinschaft

Abstract

In the Drosophila female germline, oskar messenger RNA is transported on microtubules from the nurse cells to the posterior pole of the oocyte, where it is translated. Transport of oskar transcripts from the nurse cells into the oocyte requires dynein, while localization of the mRNAs within the oocyte to the posterior pole is dependent upon kinesin-1. Staufen, a double-stranded RNA (dsRNA)-binding protein, has been shown to bind the oskar mRNA transport complex in the oocyte and inactivate dynein; however, it remains unclear how kinesin is activated. Here, using surface plasmon resonance, nuclear magnetic resonance spectroscopy, and RNA imaging within egg chambers, we demonstrate that Staufen directly interacts with Tropomyosin1-I/C (Tm1), a non-canonical kinesin adaptor. This work provides molecular evidence of how Staufen integrates into the oskar messenger ribonucleoprotein (mRNP) complex.

Further data

Item Type: Article in a journal
Keywords: RNA localization; RNA-binding proteins; motor proteins; protein-protein interactions; NMR; biophysics
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry > Chair Biochemistry IV - Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Research Institutions > Central research institutes > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Research Institutions
Research Institutions > Central research institutes
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-9101-6
Date Deposited: 10 Apr 2026 12:45
Last Modified: 10 Apr 2026 12:45
URI: https://epub.uni-bayreuth.de/id/eprint/9101

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