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TitleThe C-terminal dimerization domain of the respiratory mucin MUC5B functions in mucin stability and intracellular packaging before secretion.
Journal, issue, pagesJ Biol Chem, Vol. 294, Issue 45, Page 17105-17116, Year 2019
Publish dateNov 8, 2019
AuthorsCaroline Ridley / Michael P Lockhart-Cairns / Richard F Collins / Thomas A Jowitt / Durai B Subramani / Mehmet Kesimer / Clair Baldock / David J Thornton /
PubMed AbstractMucin 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 ...Mucin 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. Here, using cryogenic electron microscopy (cryo-EM) and small-angle X-ray scattering (SAXS) analyses of recombinant disulfide-linked dimeric MUC5B dimerization domain we identified an asymmetric, elongated twisted structure, with a double globular base. We found that the dimerization domain is more resistant to disruption than the multimerization domain suggesting the twisted structure of the dimerization domain confers additional stability to MUC5B polymers. Size-exclusion chromatography-multiangle light scattering (SEC-MALS), SPR-based biophysical analyses and microscale thermophoresis of the dimerization domain disclosed no further assembly, but did reveal reversible, calcium-dependent interactions between the dimerization and multimerization domains that were most active at acidic pH, suggesting that these domains have a role in MUC5B intragranular organization. In summary, our results suggest a role for the C-terminal dimerization domain of MUC5B in compaction of mucin chains during granular packaging via interactions with the N-terminal multimerization domain. Our findings further suggest that the less stable multimerization domain provides a potential target for mucin depolymerization to remove mucus plugs in COPD and other lung pathologies.
External linksJ Biol Chem / PubMed:31570524 / PubMed Central
MethodsEM (single particle)
Resolution7.5 - 10.0 Å
Structure data

EMDB-10264:
Respiratory mucin MUC5B; C-terminal dimerization domain structure
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-10336:
Respiratory mucin MUC5B: C-terminal dimerization domain structure
Method: EM (single particle) / Resolution: 8.9 Å

EMDB-10339:
Respiratory mucin MUC5B; C-terminal dimerization domain structure
Method: EM (single particle) / Resolution: 7.5 Å

Source
  • Homo sapiens (human)

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