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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
Open Access Gold
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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
Corresponding Author
Keywords Cp: Molecular Biology ; Nmr ; Rna Localization ; Rna-binding Proteins ; Biophysics ; Motor Proteins ; Protein-protein Interactions
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
Non-patent literature Publications
Reviewing status Peer reviewed