Literature DB >> 31338952

The multi PAM2 protein Upa2 functions as novel core component of endosomal mRNA transport.

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.
© 2019 The Authors.

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


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