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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.
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.
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.
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.
Protein kinase-mediated regulation of glucose transporters translocation to the plasma membrane
Publication . Henriques, Andreia; Matos, Paulo; 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.
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Wellcome Trust
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Immunology and Infectious Disease
Número da atribuição
106080