@article {66024,
	title = {RNA transport and local translation in neurodevelopmental and neurodegenerative disease.},
	journal = {Nature Neuroscience},
	volume = {24},
	year = {2021},
	month = {2021 May 01},
	pages = {622-32},
	abstract = {<p>Neurons decentralize protein synthesis from the cell body to support the active metabolism of remote dendritic and axonal compartments. The neuronal RNA transport apparatus, composed of cis-acting RNA regulatory elements, neuronal transport granule proteins, and motor adaptor complexes, drives the long-distance RNA trafficking required for local protein synthesis. Over the past decade, advances in human genetics, subcellular biochemistry, and high-resolution imaging have implicated each member of the apparatus in several neurodegenerative diseases, establishing failed RNA transport and associated processes as a unifying pathomechanism. In this review, we deconstruct the RNA transport apparatus, exploring each constituent{\textquoteright}s role in RNA localization and illuminating their unique contributions to neurodegeneration.</p>
},
	issn = {1546-1726},
	doi = {10.1038/s41593-020-00785-2},
	author = {Fernandopulle, Michael S and Lippincott-Schwartz, Jennifer and Ward, Michael E}
}
@article {65156,
	title = {RNA granules hitchhike on lysosomes for long-distance transport, Using annexin A11 as a molecular tether.},
	journal = {Cell},
	volume = {179},
	year = {2019},
	month = {2019 Sep 19},
	pages = {147-164.e20},
	abstract = {<p>Long-distance RNA transport enables local protein synthesis at metabolically-active sites distant from the nucleus. This process ensures an appropriate spatial organization of proteins, vital to polarized cells such as neurons. Here, we present a mechanism for RNA transport in which RNA granules "hitchhike" on moving lysosomes. In\&nbsp;vitro biophysical modeling, live-cell microscopy, and unbiased proximity labeling proteomics reveal that annexin A11 (ANXA11), an RNA granule-associated phosphoinositide-binding protein, acts as a molecular tether between RNA granules and lysosomes. ANXA11 possesses an N-terminal low complexity domain, facilitating its phase separation into membraneless RNA granules, and a C-terminal membrane binding domain, enabling interactions with lysosomes. RNA granule transport requires ANXA11, and amyotrophic lateral sclerosis (ALS)-associated mutations in ANXA11 impair RNA granule transport by disrupting their interactions with lysosomes. Thus, ANXA11 mediates neuronal RNA transport by tethering RNA granules to actively-transported lysosomes, performing a critical cellular function that is disrupted in ALS.</p>
},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2019.08.050},
	author = {Liao, Ya-Cheng and Fernandopulle, Michael S and Wang, Guozhen and Choi, Heejun and Hao, Ling and Drerup, Catherine M and Patel, Rajan and Qamar, Seema and Nixon-Abell, Jonathon and Shen, Yi and Meadows, William and Vendruscolo, Michele and Knowles, Tuomas P J and Nelson, Matthew and Czekalska, Magdalena A and Musteikyte, Greta and Gachechiladze, Mariam A and Stephens, Christina A and Pasolli, H Amalia and Forrest, Lucy R and St George-Hyslop, Peter and Lippincott-Schwartz, Jennifer and Ward, Michael E}
}
