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Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival

Standard

Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival. / Huang, Yen-Lin; Liang, Ching-Yeu; Labitzky, Vera; Ritz, Danilo; Oliveira, Tiago; Cumin, Cécile; Estermann, Manuela; Lange, Tobias; Everest-Dass, Arun V; Jacob, Francis.

In: ISCIENCE, Vol. 24, No. 10, 103168, 22.10.2021.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Huang, Y-L, Liang, C-Y, Labitzky, V, Ritz, D, Oliveira, T, Cumin, C, Estermann, M, Lange, T, Everest-Dass, AV & Jacob, F 2021, 'Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival', ISCIENCE, vol. 24, no. 10, 103168. https://doi.org/10.1016/j.isci.2021.103168

APA

Huang, Y-L., Liang, C-Y., Labitzky, V., Ritz, D., Oliveira, T., Cumin, C., Estermann, M., Lange, T., Everest-Dass, A. V., & Jacob, F. (2021). Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival. ISCIENCE, 24(10), [103168]. https://doi.org/10.1016/j.isci.2021.103168

Vancouver

Huang Y-L, Liang C-Y, Labitzky V, Ritz D, Oliveira T, Cumin C et al. Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival. ISCIENCE. 2021 Oct 22;24(10). 103168. https://doi.org/10.1016/j.isci.2021.103168

Bibtex

@article{85e57d7b1db44e3d99578ab24112a369,
title = "Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival",
abstract = "Integrin alpha 2 (ITGA2) promotes cancer metastasis through selective adhesion to ECM proteins; however, the specific contribution of integrin glycosylation remains uncertain. We provide evidence that ITGA2 is a highly glycosylated transmembrane protein expressed in ovarian cancer tissue and cell lines. In-depth glycoproteomics identified predominant N- and O-glycosylation sites harboring substantially divergent ITGA2 glycosylation profiles. Generated putative ITGA2 N-glycosite mutants halted collagen and laminin binding and cells lacking N-glycosylated ITGA2 were marginally adherent to collagen, likely associated with its enhanced proteasome degradation through poly-ubiquitination. Proteomic and enrichment pathway analysis revealed increased cellular apoptosis and collagen organization in non-glycosylated ITGA2 mutant cells. Moreover, we provide evidence that ITGA2-specific sialylation is involved in selective cell-ECM binding. These results highlight the importance of glycans in regulating ITGA2 stability and ligand binding capacity which in turn modulates downstream focal adhesion and promotes cell survival in a collagen environment.",
author = "Yen-Lin Huang and Ching-Yeu Liang and Vera Labitzky and Danilo Ritz and Tiago Oliveira and C{\'e}cile Cumin and Manuela Estermann and Tobias Lange and Everest-Dass, {Arun V} and Francis Jacob",
note = "{\textcopyright} 2021 The Author(s).",
year = "2021",
month = oct,
day = "22",
doi = "10.1016/j.isci.2021.103168",
language = "English",
volume = "24",
journal = "ISCIENCE",
issn = "2589-0042",
publisher = "Elsevier Inc.",
number = "10",

}

RIS

TY - JOUR

T1 - Site-specific N-glycosylation of integrin α2 mediates collagen-dependent cell survival

AU - Huang, Yen-Lin

AU - Liang, Ching-Yeu

AU - Labitzky, Vera

AU - Ritz, Danilo

AU - Oliveira, Tiago

AU - Cumin, Cécile

AU - Estermann, Manuela

AU - Lange, Tobias

AU - Everest-Dass, Arun V

AU - Jacob, Francis

N1 - © 2021 The Author(s).

PY - 2021/10/22

Y1 - 2021/10/22

N2 - Integrin alpha 2 (ITGA2) promotes cancer metastasis through selective adhesion to ECM proteins; however, the specific contribution of integrin glycosylation remains uncertain. We provide evidence that ITGA2 is a highly glycosylated transmembrane protein expressed in ovarian cancer tissue and cell lines. In-depth glycoproteomics identified predominant N- and O-glycosylation sites harboring substantially divergent ITGA2 glycosylation profiles. Generated putative ITGA2 N-glycosite mutants halted collagen and laminin binding and cells lacking N-glycosylated ITGA2 were marginally adherent to collagen, likely associated with its enhanced proteasome degradation through poly-ubiquitination. Proteomic and enrichment pathway analysis revealed increased cellular apoptosis and collagen organization in non-glycosylated ITGA2 mutant cells. Moreover, we provide evidence that ITGA2-specific sialylation is involved in selective cell-ECM binding. These results highlight the importance of glycans in regulating ITGA2 stability and ligand binding capacity which in turn modulates downstream focal adhesion and promotes cell survival in a collagen environment.

AB - Integrin alpha 2 (ITGA2) promotes cancer metastasis through selective adhesion to ECM proteins; however, the specific contribution of integrin glycosylation remains uncertain. We provide evidence that ITGA2 is a highly glycosylated transmembrane protein expressed in ovarian cancer tissue and cell lines. In-depth glycoproteomics identified predominant N- and O-glycosylation sites harboring substantially divergent ITGA2 glycosylation profiles. Generated putative ITGA2 N-glycosite mutants halted collagen and laminin binding and cells lacking N-glycosylated ITGA2 were marginally adherent to collagen, likely associated with its enhanced proteasome degradation through poly-ubiquitination. Proteomic and enrichment pathway analysis revealed increased cellular apoptosis and collagen organization in non-glycosylated ITGA2 mutant cells. Moreover, we provide evidence that ITGA2-specific sialylation is involved in selective cell-ECM binding. These results highlight the importance of glycans in regulating ITGA2 stability and ligand binding capacity which in turn modulates downstream focal adhesion and promotes cell survival in a collagen environment.

U2 - 10.1016/j.isci.2021.103168

DO - 10.1016/j.isci.2021.103168

M3 - SCORING: Journal article

C2 - 34646995

VL - 24

JO - ISCIENCE

JF - ISCIENCE

SN - 2589-0042

IS - 10

M1 - 103168

ER -