Fibro-adipogenic progenitors in skeletal muscle contribute to the neuromuscular pathogenesis of spinal muscular atrophy, and depletion of SMN in chondrocytes reduces local IGF sigaling in growth plate.

The identification of SMA-miR supports the pathogenic role of skeletal muscle in spinal muscular atrophy and, integrated in the SMA-score, may help to improve the phenotypic prediction for patients.

Sin1, a regulatory subunit of TOR protein kinase, has an evolutionarily conserved domain that specifically binds and recruits substrate for phosphorylation, and may represent a potential target for anti-cancer drugs.

In invertebrate and vertebrate models of Spinal Muscular Atrophy, diminished SMN protein causes Gemin3-dependent decreases in microRNA function, leading to upregulated M2 muscarinic receptor and deleterious consequences.

The nuclear membrane protein SUN1 stabilizes endothelial cell-cell junctions far from the nucleus via regulation of microtubule dynamics and Rho GEF-H1 signaling, revealing long-range cellular communication important for vascular development and function.

The structural model of hnRNP A1 shows that it can bind with both RRMs to RNA, which is shown to be relevant for the SMN2 exon 7 splicing mechanism in vivo.

Structures of human SMG1-9 and SMG1-8-9 reveal how the SMG1 kinase active site is targeted by a specific inhibitor and provide insights into the regulation of the SMG1-8-9 kinase complex in nonsense-mediated mRNA decay.

First structural view of a substrate-bound PIKK (PI3K-related-kinase) by cryo-EM explains phosphorylation specificity toward a short amino-acid motif shared across the PIKK family and rationalizes PIKK auto-inhibition by regulatory domain.

Interactions with Sm proteins can provide a way in which regulatory factors can modulate alternative splice site choices.