Newmarket Scientific
Newmarket Scientific

NEWS: RNA-binding Proteins and Stress granules in ALS-FTD

Cytoplasmic stress granules are membrane-less aggregates that form through liquid phase separation as a protective response to physiological or pathological conditions such as oxidative stress, hypoxia or virus infection. They are transient and usually disappear after the stress is removed.


Stress granules are mainly composed of messenger RNAs (mRNAs) stalled in translation initiation, translation initiation components such as eukaryotic initiation factor 4G (eIF4G), RNA-binding proteins (RBPs) and ribonucleoproteins. Formation of stress granules can be initiated by the Ras GTPase-activating protein-binding protein 1 (G3BP1), which is commonly used as a stress granule marker.


Mutations in genes that encode RNA binding proteins (RBPs) such as FUS/TLS, TDP-43, Ataxin 2, TAF15, EWSR1, hnRNPA1 and hnRNPA2, MATR3 and TIA-1 have recently been linked to ALS/FTD. Some of these RNA binding proteins contain low complexity sequence domains (LCDs) that have been shown to mediate the phase separation. Mutations found in these domains increase the propensity of RNA binding proteins to aggregate and form pathological amyloid-like fibrils in the cell bodies.


The links above detail antibodies available to each stress granule protein, but we have antibodies to many more related proteins with further antibodies in devlopment, so please search for your antibody using the search box at the top of the page, or complete the form below to request a sample of any antibody mentioned.



Related products and news items:

USP10   Caprin1    HDAC6    eIF4A3


TDP43 - TAR DNA-binding protein 43: A key protein in ALS and FTLD, Parkinson's and Alzheimer's 




References: RNA-Binding Proteins in Amyotrophic Lateral Sclerosis, Zhao M. et al.

Mol Cells. 2018 Sep 30;41(9):818-829  


Decoding ALS: From Genes to Mechanism, Taylor JP et al.

Nature. 2016 Nov 10; 539(7628): 197–206.


Relationships between Stress Granules, Oxidative Stress, and Neurodegenerative Diseases Chen L et al.  Oxidative Medicine and Cellular Longevity, Volume 2017, Article ID 1809592



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