Journal Article

PUBDB-2024-01774

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The structure of the second CysD domain of MUC2 and role in mucin organization by transglutaminase-based cross-linking

Recktenwald, C. V. (Corresponding author) ; Karlsson, G. ; Garcia-Bonete, M.-J. ; Katona, G. ; Jensen, M. ; Lymer, R. ; Bäckström, M. ; Johansson, M. E. V. ; Hansson, G. C. (Corresponding author) ; Trillo-Muyo, S. (Corresponding author)

2024
Elsevier [New York, NY]

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Please use a persistent id in citations: doi:10.1016/j.celrep.2024.114207  doi:10.3204/PUBDB-2024-01774

Abstract: The MUC2 mucin protects the colonic epithelium by a two-layered mucus with an inner attached bacteria-free layer and an outer layer harboring commensal bacteria. CysD domains are 100 amino-acid-long sequences containing 10 cysteines that separate highly O-glycosylated proline, threonine, serine (PTS) regions in mucins. The structure of the second CysD, CysD2, of MUC2 is now solved by nuclear magnetic resonance. CysD2 shows a stable stalk region predicted to be partly covered by adjacent O-glycans attached to neighboring PTS sequences, whereas the CysD2 tip with three flexible loops is suggested to be well exposed. It shows transient dimer interactions at acidic pH, weakened at physiological pH. This transient interaction can be stabilized in vitro and in vivo by transglutaminase 3-catalyzed isopeptide bonds, preferring a specific glutamine residue on one flexible loop. This covalent dimer is modeled suggesting that CysD domains act as connecting hubs for covalent stabilization of mucins to form a protective mucus.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2024

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