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Title: Human asparagine synthetase associates with the mitotic spindle
Authors: Chalongrat Noree
Monfort, Elena
Vorasuk Shotelersuk
Email: No information provided
No information provided
Other author: Chulalongkorn University. Faculty of Medicine
Issue Date: 14-Dec-2018
Publisher: The Company of Biologists Ltd
Citation: Biology Open. Vol.7, Issue 12 (Dec, 2018), 7 pages
Abstract: Cancer cells are characterized by extensive reprogramming of metabolic pathways in order to promote cell division and survival. However, the growth promotion effects of metabolic reprogramming can be due to moonlighting functions of metabolic enzymes as well as the redirection of flux through particular pathways. To identify metabolic enzymes that might have potential moonlighting functions in oncogenesis, we have examined recent screens of the yeast GFP strain collection for metabolic enzymes that have been implicated in cancer metabolism with an unusual subcellular localization. Asparagine synthetase forms filaments in yeast in response to nutrient limitation and is part of a pathway that is a chemotherapy target in acute lymphoblastic leukemia. Interestingly, while yeast asparagine synthetase forms cytoplasmic filaments in response to nutrient stress, human asparagine synthetase is associated with the centrosomes and mitotic spindles. This localization is disrupted by both nocodazole and asparaginase treatments. This failure to localize occurs even though asparagine synthetase is highly upregulated in response to asparaginase treatment. Together, these results argue that human asparagine synthetase undergoes regulated recruitment to the mitotic spindles and that it may have acquired a second role in mitosis similar to other metabolic enzymes that contribute to metabolic reprogramming in cancer cells.
ISSN: 2046-6390
metadata.dc.identifier.DOI: 10.1242/bio.038307
Type: Article
Appears in Collections:Chula Scholars - 2018

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