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Glycobiology and Extracellular Matrices
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- Glycobiology and Extracellular MatricesOpen Access
The C-terminal dimerization domain of the respiratory mucin MUC5B functions in mucin stability and intracellular packaging before secretion
Journal of Biological ChemistryVol. 294Issue 45p17105–17116Published online: September 30, 2019- Caroline Ridley
- Michael P. Lockhart-Cairns
- Richard F. Collins
- Thomas A. Jowitt
- Durai B. Subramani
- Mehmet Kesimer
- and others
Cited in Scopus: 14Mucin 5B (MUC5B) has an essential role in mucociliary clearance that protects the pulmonary airways. Accordingly, knowledge of MUC5B structure and its interactions with itself and other proteins is critical to better understand airway mucus biology and improve the management of lung diseases such as asthma, cystic fibrosis, and chronic obstructive pulmonary disease (COPD). The role of an N-terminal multimerization domain in the supramolecular organization of MUC5B has been previously described, but less is known about its C-terminal dimerization domain.