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Articles by Veronica Ryan
Messenger RNA transport on lysosomal vesicles maintains axonal mitochondrial homeostasis and prevents axonal degeneration - Nature Neuroscience
Abstract In neurons, RNA granules are transported along the axon for local translation away from the soma. Recent studies indicate that some of this transport involves hitchhiking of RNA granules on lysosome-related vesicles. In the present study, we leveraged the ability to prevent transport of these vesicles into the axon by knockout of the lysosome–kinesin adaptor BLOC-one-related complex (BORC) to identify a subset of axonal mRNAs that depend on lysosome-related vesicles for transport.
Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration
Abstract mRNA transport in neurons requires formation of transport granules containing many protein components, and subsequent alterations in phosphorylation status can release transcripts for translation. Further, mutations in a structurally disordered domain of the transport granule protein hnRNPA2 increase its aggregation and cause hereditary proteinopathy of neurons, myocytes, and bone.
Physiological, Pathological, and Targetable Membraneless Organelles in Neurons
Al-Husini N. et al. α-Proteobacterial RNA degradosomes assemble liquid–liquid phase-separated RNP bodies. Mol. Cell. 2018; 71: 1027-1039 Brangwynne C.P. et al. Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc. Natl. Acad. Sci. U. S. A. 2011; 108: 4334-4339 Feric M. et al. Coexisting liquid phases underlie nucleolar subcompartments. Cell. 2016; 165: 1686-1697 Hennig S. et al.
The SH3 domain of Fyn kinase interacts with and induces liquid-liquid phase separation of the low-complexity domain of hnRNPA2
Joshua Amaya‡12, Veronica H. Ryan§13 and Nicolas L. Fawzi‡4 From the ‡Department of Molecular Pharmacology, Physiology, and Biotechnology and the §Graduate Program in Neuroscience, Brown University, Providence, Rhode Island 02912 ↵4 To whom correspondence should be addressed: Dept. of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, RI 02912. Tel.: 401-863-5232; Fax: 401-863-6087; E-mail: nicolas_fawzi{at}brown.edu. ↵1 Both authors contributed equally to this work.
The SH3 domain of Fyn kinase interacts with and induces liquid-liquid phase separation of the low complexity domain of hnRNPA2
Liquid-liquid phase separation of proteins and nucleic acids into membraneless organelles (MLOs) spatially organizes cellular components and reactions. The RNA-binding protein heterogeneous nuclear ribonucleoprotein A2 (hnRNPA2) carries mRNA targets in MLOs called transport granules in neurons and oligodendrocytes. At sites of local translation, hnRNPA2 is phosphorylated by the tyrosine protein kinase Fyn, releasing the mRNA for translation. Fyn recognizes targets through its SH3 domain (Fyn-SH3).
Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation
hnRNPA2, a component of RNA-processing membraneless organelles, forms inclusions when mutated in a syndrome characterized by the degeneration of neurons (bearing features of amyotrophic lateral sclerosis [ALS] and frontotemporal dementia), muscle, and bone. Here we provide a unified structural view of hnRNPA2 self-assembly, aggregation, and interaction and the distinct effects of small chemical changes—disease mutations and arginine methylation—on these assemblies.
Young Ned by Brett Ross
I have just finished reading an awesome book from a new Australian author, Brett Ross. ‘Young Ned’ is an absorbing tale of a turning point in a young man’s life. Disillusioned and disappointed with his life in an Australian coastal town, Ned and a couple of friends embark on an adventure through Southern California, Mexico and Central America.
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