MassIVE MSV000097524

Partial Public PXD062594

O-mannose glycosylations influence E-cadherin protein interactions

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Description

Cadherins are plasma membrane adhesion molecules that play critical roles in maintaining cell-cell adhesion and modulating cell signaling during development. Their functions are mediated by extracellular cadherin (EC) domains, which facilitate adhesive interactions and enable the formation of cis- and trans assemblies at adherens junctions and desmosomes. The EC domains adopt a characteristic immunoglobulin-like fold composed of seven beta-strands (A-G), and are further modified by N-linked and O-linked glycosylation, including alpha-linked mannose monosaccharides (O-Man) on conserved serine and threonine residues of B- and G-strands. EC domain O-Man glycosylation is catalyzed by TMTC enzymes: TMTC3 catalyzes modifications to the G-strands, whereas TMTC2 targets the B-strands. Given the site-specific deposition of O-Man glycans by dedicated enzymes and the central role of EC domains in cadherins functions, we hypothesized that these PTMs may fine-tune cellular adhesion strength and otherwise contribute to diverse physical interactions that involve cadherins. To test these hypotheses, we assayed for changes in protein-protein interactions formed with epithelial (E)-cadherin in model cells where O-Man PTMs were genetically ablated. Herein, we report O-Man-dependent, E-cadherin (CDH1) protein interactions, revealed by affinity proteomics; we orthogonally validate an altered association between CDH1 and CDH3 (P-cadherin), and demonstrate loss-of-function consequences of O-Man ablation on specific positions, highlighting the importance of these PTMs in cadherin-mediated adhesion. These findings provide new insights into how post-translational modifications regulate cadherin-dependent adhesion complexes. [doi:10.25345/C5QN5ZQ3X] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: E-cadherin interactome ; IP screening ; O-Man glycosyaltion ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		John LaCava, Laboratory of Cellular and Structural Biology, The Rockefeller University, USA
Submitting User: shaoshuai
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