Membrane curvature regulates the spatial distribution of bulky glycoproteins

Chih-Hao Lu, Kayvon Pedram, Ching-Ting Tsai, Taylor Jones, Xiao Li, Melissa L. Nakamoto, Carolyn R. Bertozzi and Bianxiao Cui ()
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Chih-Hao Lu: Department of Chemistry, Stanford University
Kayvon Pedram: Department of Chemistry, Stanford University
Ching-Ting Tsai: Department of Chemistry, Stanford University
Taylor Jones: Department of Chemistry, Stanford University
Xiao Li: Department of Chemistry, Stanford University
Melissa L. Nakamoto: Department of Chemistry, Stanford University
Carolyn R. Bertozzi: Department of Chemistry, Stanford University
Bianxiao Cui: Department of Chemistry, Stanford University

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract The glycocalyx is a shell of heavily glycosylated proteins and lipids distributed on the cell surface of nearly all cell types. Recently, it has been found that bulky transmembrane glycoproteins such as MUC1 can modulate membrane shape by inducing membrane protrusions. In this work, we examine the reciprocal relationship of how membrane shape affects MUC1’s spatial distribution on the cell membrane and its biological significance. By employing nanopatterned surfaces and membrane-sculpting proteins to manipulate membrane curvature, we show that MUC1 avoids positively-curved membranes (membrane invaginations) and accumulates on negatively-curved membranes (membrane protrusions). MUC1’s curvature sensitivity is dependent on the length and the extent of glycosylation of its ectodomain, with large and highly glycosylated forms preferentially staying out of positive curvature. Interestingly, MUC1’s avoidance of positive membrane curvature enables it to escape from endocytosis and being removed from the cell membrane. These findings also suggest that the truncation of MUC1’s ectodomain, often observed in breast and ovarian cancers, may enhance its endocytosis and potentiate its intracellular accumulation and signaling.

Date: 2022
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DOI: 10.1038/s41467-022-30610-2

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