| Literature DB >> 31338952 |
Silke Jankowski1, Thomas Pohlmann1, Sebastian Baumann1, Kira Müntjes1, Senthil Kumar Devan1, Sabrina Zander1, Michael Feldbrügge1.
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.Entities:
Keywords: MLLE domain; PAM2 motif; endosome; microtubule; poly(A)-binding protein
Mesh:
Substances:
Year: 2019 PMID: 31338952 PMCID: PMC6726905 DOI: 10.15252/embr.201847381
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807