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Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

ABSTRACT: Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signaling. However, the function of tensin-2 beyond localizing to focal adhesions remain poorly understood. We utilized proximity-dependent biotinylation and strep-tag affinity proteomics to identify interaction partners of tensin-2 in HEK293 cells. Interactomics linked tensin-2 to known focal adhesion proteins and the dystrophin glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in HEK293 and MEF cells and found that pY483 tensin-2 is enriched in adhesions in MEF cells. Our study unveils novel interaction partners for tensin-2 and further solidifies its speculated role in cell energy metabolism. These findings shed fresh insight on the functions of tensin-2, highlighting its potential as a therapeutic target for diseases associated with impaired cell adhesion and metabolism.

ORGANISM(S): Homo sapiens

PROVIDER: GSE231782 | GEO | 2024/07/20

REPOSITORIES: GEO

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Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

Project description:Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signalling. However, its functions beyond localizing to focal adhesions remain poorly understood. To identify tensin-2's interaction partners in HEK293 cells, we utilized proximity-dependent biotinylation and strep-tag affinity proteomics. Results linked tensin-2 to known focal adhesion proteins and the dystrophin-glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in HEK293 and MEF cells, as well as gene expression in HEK293 cells. Of note, Y483-phosphorylation directs tensin-2 to adhesion sites in MEF cells. Our study unveils numerous novel interaction partners for tensin-2, further solidifies its speculated role in cell energy metabolism and identifies Y483-phosphorylation as a crucial regulator for tensin-2 localization. These findings shed fresh insight into the functions of tensin-2, highlighting its potential as a therapeutic target for diseases associated with impaired cell adhesion and metabolism.

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Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

Project description:Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

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