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SMN affects membrane remodelling and anchoring of the protein synthesis machinery.

Journal of cell science (2016-01-09)
Francesca Gabanella, Cinzia Pisani, Antonella Borreca, Stefano Farioli-Vecchioli, Maria Teresa Ciotti, Tiziano Ingegnere, Annalisa Onori, Martine Ammassari-Teule, Nicoletta Corbi, Nadia Canu, Lucia Monaco, Claudio Passananti, Maria Grazia Di Certo

Disconnection between membrane signalling and actin networks can have catastrophic effects depending on cell size and polarity. The survival motor neuron (SMN) protein is ubiquitously involved in assembly of spliceosomal small nuclear ribonucleoprotein particles. Other SMN functions could, however, affect cellular activities driving asymmetrical cell surface expansions. Genes able to mitigate SMN deficiency operate within pathways in which SMN can act, such as mRNA translation, actin network and endocytosis. Here, we found that SMN accumulates at membrane protrusions during the dynamic rearrangement of the actin filaments. In addition to localization data, we show that SMN interacts with caveolin-1, which mediates anchoring of translation machinery components. Importantly, SMN deficiency depletes the plasma membrane of ribosomes, and this correlates with the failure of fibroblasts to extend membrane protrusions. These findings strongly support a relationship between SMN and membrane dynamics. We propose that SMN could assembly translational platforms associated with and governed by the plasma membrane. This activity could be crucial in cells that have an exacerbated interdependence of membrane remodelling and local protein synthesis.

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