The structure of the second CysD domain of MUC2 and role in mucin organization by transglutaminase-based cross-linking

Recktenwald, Christian V.; Karlsson, Göran; Garcia-Bonete, Maria-Jose; Katona, Gergely; Jensen, Maja; Lymer, Richard; Bäckström, Malin; Johansson, Malin E.V.; Hansson, Gunnar C.; Trillo-Muyo, Sergio

doi:10.1016/j.celrep.2024.114207

Cell Reports

2024

DOI: 10.1016/j.celrep.2024.114207

|View full text |Cite

The structure of the second CysD domain of MUC2 and role in mucin organization by transglutaminase-based cross-linking

Christian V. Recktenwald,

Göran Karlsson,

Maria-Jose Garcia-Bonete

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Preprint1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Structural mechanism of MUC5AC mucin net-like polymer formation and its SNP variability that affect risk of the lung diseases COPD and IPF

Trillo-Muyo,

Ermund,

Magnusson

et al. 2024

Preprint

View full text Add to dashboard Cite

Gel-forming mucins MUC5AC and MUC5B constitute the main structural component of the mucus in the respiratory system. Secreted mucins interact specifically with each other and other molecules giving mucus specific properties. We determined the cryoEM structures of the wild type MUC5AC-D3 assembly and the structural SNP variants R996Q and R1201W. Our structures explain the basis of MUC5AC N-terminal non-covalent oligomerization upon secretion. The MUC5AC-D3 assembly forms covalent dimers in two alternative conformations, open and closed. The closed conformation dimers interact through an arginine rich loop in the TIL3 domain forming tetramers. Moreover, we found a positive disease correlation between the SNP (R996Q, rs878913005), Chronic Obstructive Pulmonary Disease (COPD), and Idiopathic Pulmonary Fibrosis (IPF). The well-known MUC5B promotor SNP (rs35705950) association with IPF is much stronger when combined with the MUC5AC SNP. Our study provides a model to explain the formation of MUC5AC net-like structures and how both SNPs will affect mucus organization and increase risk of lung disease.

show abstract

Structural mechanism of MUC5AC mucin net-like polymer formation and its SNP variability that affect risk of the lung diseases COPD and IPF

Trillo-Muyo,

Ermund,

Magnusson

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

The structure of the second CysD domain of MUC2 and role in mucin organization by transglutaminase-based cross-linking

Cited by 1 publication

References 44 publications

Structural mechanism of MUC5AC mucin net-like polymer formation and its SNP variability that affect risk of the lung diseases COPD and IPF

Structural mechanism of MUC5AC mucin net-like polymer formation and its SNP variability that affect risk of the lung diseases COPD and IPF

Contact Info

Product

Resources

About