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UID:1017@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20211206T130000

DTEND;TZID=Asia/Jerusalem:20211206T140000

DTSTAMP:20211201T140946Z

URL:https://biology.technion.ac.il/en/seminars/prof-debora-fass-department
 -of-chemical-and-structural-biology-weizmann-institute-of-science/

SUMMARY:Prof. Debora Fass\, Department of Chemical and Structural Biology\,
  Weizmann Institute of Science [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n Title: Golgi Redox and G
 ut Health: the Elegant Mechanism for ConstructingIntestinal MucusGuest: De
 borah Fass\, Departmentof Chemical and Structural Biology\, WeizmannInstit
 ute of Science AbstractThreats to the body’s physical integrity come in
  a varietyof forms: pathogens\, chemical poisons and irritants\, and mecha
 nical injuries.Early in animal development\, a multifunctional safety net 
 evolved to protectagainst such hazards. This safety net is built of the mu
 cus hydrogels that coverand shield the hundreds of square meters of vulner
 able epithelia in the body\,most notably in the lungs and intestines. Mucu
 s forms by disulfide bond cross-linkingof enormous glycoproteins called 
 “mucins.” Using X-ray crystallography andcryo-electron microscopy\, we
  determined structures of the region of theintestinal mucin involved in cr
 oss-linking. These structures revealed how themucus scaffold is organized 
 and led us to the discovery that mucus protectsagainst even more dangers t
 han was previously appreciated. In parallel\, wefound that a catalyst of d
 isulfide bond formation in the Golgi apparatus isnecessary for constructin
 g functional mucus\, but\, surprisingly\, not for carryingout the actual c
 ross-linking. Instead\, disulfide bonding in the Golgicontributes to mucus
  functionality in an unexpected manner\, revealing a newcell biological pr
 inciple likely to be relevant to other processes in additionto mucus produ
 ction.Host: Sagi Levy 

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