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The multi PAM2 protein Upa2 functions as novel core component of endosomal mRNA transport
Silke Jankowski1, Thomas Pohlmann1, Sebastian Baumann1
1Institute for Microbiology, Cluster of Excellence on Plant Sciences, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Abstract:
mRNA transport determines spatiotemporal protein expression. Transport units are higher-order ribonucleoprotein complexes containing cargo mRNAs, RNA-binding proteins and accessory proteins. Endosomal mRNA transport in fungal hyphae belongs to the best-studied translocation mechanisms. Although several factors are known, additional core components are missing. Here, we describe the 232 kDa protein Upa2 containing multiple PAM2 motifs (poly[A]-binding protein [Pab1]-associated motif 2) as a novel core component. Loss of Upa2 disturbs transport of cargo mRNAs and associated Pab1. Upa2 is present on almost all transport endosomes in an mRNA-dependent manner. Surprisingly, all four PAM2 motifs are dispensable for function during unipolar hyphal growth. Instead, Upa2 harbours a novel N-terminal effector domain as important functional determinant as well as a C-terminal GWW motif for specific endosomal localisation. In essence, Upa2 meets all the criteria of a novel core component of endosomal mRNA transport and appears to carry out crucial scaffolding functions.
Insights
Researchers identified Upa2, a novel protein essential for mRNA transport in fungal hyphae. This protein acts as a scaffold, ensuring proper protein expression by facilitating the movement of messenger RNA (mRNA) and associated proteins.
Area of Science:
- Molecular Biology
- Cell Biology
- Mycology
Background:
- Spatiotemporal protein expression is regulated by mRNA transport.
- mRNA transport occurs via ribonucleoprotein complexes.
- Endosomal mRNA transport in fungal hyphae is a well-studied mechanism with known components, but gaps remain.
Purpose of the Study:
- To identify novel core components of endosomal mRNA transport in fungal hyphae.
- To characterize the function and localization of the newly identified protein, Upa2.
Main Methods:
- Protein identification and characterization.
- Analysis of Upa2's role in mRNA and protein Pab1 transport.
- Localization studies of Upa2 on endosomes.
- Functional assays during hyphal growth.
Main Results:
- A novel 232 kDa protein, Upa2, containing multiple PAM2 motifs was identified as a core component.
- Loss of Upa2 disrupts the transport of cargo mRNAs and Pab1.
- Upa2 localizes to transport endosomes in an mRNA-dependent manner.
- PAM2 motifs are dispensable for Upa2 function; an N-terminal effector domain and C-terminal GWW motif are crucial for function and localization, respectively.
Conclusions:
- Upa2 is a novel core component of endosomal mRNA transport in fungal hyphae.
- Upa2 plays a crucial scaffolding role in this process.
- Specific domains of Upa2 mediate its function and localization, independent of its PAM2 motifs.
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