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New insights into how cancer cells regulate glucose uptake by protein phosphorylation

Publication . Henriques, Andreia; Jordan, Peter

Cancer cells require increased glucose supply to sustain proliferation. One mechanism involves increased expression of glucose transporter (GLUT) genes. But insulin has revealed that protein phosphorylation is another key mechanism in glucose uptake regulation: insulin binding to responsive cells triggers a signalling cascade with phosphorylation of TBC1D4, a negative regulator of endosomal GLUT trafficking, so that more transporters are inserted into the plasma membrane.

2017-05-08Conference object

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Protein kinase-mediated plasma membrane translocation of glucose transporters in cancer cells

Publication . Henriques, Andreia; Jordan, Peter

Cancer cells require increased glucose supply to sustain proliferation. One mechanism involves increased expression of glucose transporter (GLUT) genes.

2017-06-01Conference object

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Regulation of glucose transporters by protein kinases in cancer cells

Publication . Henriques, Andreia; Matos, Paulo; Jordan, Peter

Background: Cancer cells require increased glucose supply to sustain proliferation. One mechanism involves increased expression of glucose transporter (GLUT) genes. But insulin has revealed that protein phosphorylation is another key mechanism in glucose uptake regulation: insulin binding to responsive cells triggers a signalling cascade with phosphorylation of TBC1D4, a negative regulator of endosomal GLUT trafficking, so that more transporters are inserted into the plasma membrane. Previous work from the host lab has identified the family of WNK protein kinases and shown that WNK1 can also phosphorylate TBC1D4 and promote GLUT translocation to the cell surface. Our objective is to understand the contribution of WNK1 to glucose uptake in colorectal cancer cells.

2017-09-08Conference object

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Regulation of glucose uptake in mammalian cells by protein phosphorylation

Publication . Henriques, Andreia; Jordan, Peter

Cancer cells demand increased amounts of glucose to sustain their proliferation and upregulate plasma membrane expression of glucose transporter GLUT1. In insulin responsive cells, glucose uptake requires previous phosphorylation of TBC1D4, a negative regulator of endosomal GLUT traffic. Previous work published by the host lab has discovered that protein kinase WNK1 can also phosphorylate TBC1D4 and promote the translocation of GLUT1 to the cell surface.

2017-06-18Conference object

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Protein kinase-mediated regulation of glucose transporters translocation to the plasma membrane

Publication . Henriques, Andreia; Matos, Paulo; Jordan, Peter

2018-09Conference object

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