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Gaber, T.* ; Monecke, T.* ; Grabowski, J.* ; Simon, B.* ; Williams, T.* ; Roman, V. ; Chao, J.* ; Hennig, J.* ; Ephrussi, A.* ; Niessing, D. ; Heber, S.D.*

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

Cell Rep. 44:115906 (2025)
Publ. Version/Full Text Research data DOI PMC
Creative Commons Lizenzvertrag
Open Access Green as soon as Postprint is submitted to ZB.
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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Cp: Molecular Biology ; Nmr ; Rna Localization ; Rna-binding Proteins ; Biophysics ; Motor Proteins ; Protein-protein Interactions; Translational Regulation; Localization; Tropomyosin; Kinesin-1; Egalitarian; Reveals; Domains; Signals; Chain
Language english
Publication Year 2025
HGF-reported in Year 2025
ISSN (print) / ISBN 2211-1247
e-ISSN 2211-1247
Journal Cell Reports
Quellenangaben Volume: 44, Issue: 7, Pages: , Article Number: 115906 Supplement: ,
Publisher Cell Press
Publishing Place 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status Peer reviewed
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503091-001
Grants EMBL
DFG
Deutsche Forschungsgemeinschaft (DFG)
EMBL Interdisciplinary Postdoctoral fellowship (EIPOD) Program under Marie Curie Cofund Actions MSCA-COFUND-FP
Scopus ID 105008809191
PubMed ID 40570376
Erfassungsdatum 2025-06-27