TY - JOUR

T1 - Amyloid Fibrils of the s36 Protein Modulate the Morphogenesis of Drosophila melanogaster Eggshell

AU - Валина, Анна Алексеевна

AU - Синюкова , Вера Александровна

AU - Белашова, Татьяна Алексеевна

AU - Канапин, Александр Артурович

AU - Самсонова, Анастасия Александровна

AU - Машарский, Алексей Эльвинович

AU - Лыхолай, Анна Николаевна

AU - Галкина, Светлана Анатольевна

AU - Задорский, Сергей Павлович

AU - Галкин, Алексей Петрович

PY - 2024/11/21

Y1 - 2024/11/21

N2 - Drosophila melanogaster is the oldest classic model object in developmental genetics. It may seem that various structures of the fruit fly at all developmental stages have been well studied and described. However, recently we have shown that some specialized structures of the D. melanogaster eggshell contain an amyloid fibril network. Here, we demonstrate that this amyloid network is formed by the chorionic protein s36. The s36 protein colocalizes with the amyloid-specific dyes Congo Red and Thioflavin S in the micropyle, dorsal appendages, and pillars. The fibrils of s36 obtained from the eggs demonstrate amyloid properties. In the context of the CG33223 gene deletion, the s36 protein is produced but is not detected in the eggshell. The absence of amyloid fibrils of s36 in the eggshell disrupts the endochorion morphology and blocks the development of the micropyle, dorsal appendages, and pillars, leading to sterility. Our data show for the first time that amyloid fibrils are essential for morphogenesis modulation. We suggest that attachment of follicle cells to the s36 extracellular fibrils triggers signaling to enable subsequent cellular divisions needed for building the specialized eggshell structures.

AB - Drosophila melanogaster is the oldest classic model object in developmental genetics. It may seem that various structures of the fruit fly at all developmental stages have been well studied and described. However, recently we have shown that some specialized structures of the D. melanogaster eggshell contain an amyloid fibril network. Here, we demonstrate that this amyloid network is formed by the chorionic protein s36. The s36 protein colocalizes with the amyloid-specific dyes Congo Red and Thioflavin S in the micropyle, dorsal appendages, and pillars. The fibrils of s36 obtained from the eggs demonstrate amyloid properties. In the context of the CG33223 gene deletion, the s36 protein is produced but is not detected in the eggshell. The absence of amyloid fibrils of s36 in the eggshell disrupts the endochorion morphology and blocks the development of the micropyle, dorsal appendages, and pillars, leading to sterility. Our data show for the first time that amyloid fibrils are essential for morphogenesis modulation. We suggest that attachment of follicle cells to the s36 extracellular fibrils triggers signaling to enable subsequent cellular divisions needed for building the specialized eggshell structures.

KW - Amyloid/metabolism

KW - Animals

KW - Drosophila Proteins/metabolism

KW - Drosophila melanogaster/metabolism

KW - Egg Proteins/metabolism

KW - Egg Shell/metabolism

KW - Female

KW - Morphogenesis/genetics

KW - sterility

KW - Drosophila

KW - eggshell

KW - functional amyloid

KW - chorion

KW - morphogenesis

KW - s36

KW - gene CG33223

UR - https://www.mendeley.com/catalogue/a1bca41f-0e62-3946-b54f-fd86a8f43492/

U2 - 10.3390/ijms252312499

DO - 10.3390/ijms252312499

M3 - Article

C2 - 39684212

VL - 25

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 23

M1 - 12499

ER -