Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo. / Данилов, Лаврентий Глебович; Москаленко, Светлана Евгеньевна; Матвеенко, Андрей Георгиевич; Суханова, Ксения Владимировна; Белоусов, Михаил Владимирович; Журавлева, Галина Анатольевна; Бондарев, Станислав Александрович.
в: Biomedicines, Том 9, № 10, 1451, 13.10.2021.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo
AU - Данилов, Лаврентий Глебович
AU - Москаленко, Светлана Евгеньевна
AU - Матвеенко, Андрей Георгиевич
AU - Суханова, Ксения Владимировна
AU - Белоусов, Михаил Владимирович
AU - Журавлева, Галина Анатольевна
AU - Бондарев, Станислав Александрович
N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/10/13
Y1 - 2021/10/13
N2 - Amyloids are fibrillar protein aggregates with a cross-β structure and unusual features, including high resistance to detergent or protease treatment. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Several examples of nucleoporins (e.g., yeast Nup49, Nup100, Nup116, and human NUP153) are supposed to form amyloid fibrils. In this study, we demonstrated an ability of the human NUP58 nucleoporin to form amyloid aggregates in vivo and in vitro. Moreover, we found two forms of NUP58 aggregates: oligomers and polymers stabilized by disulfide bonds. Bioinformatic analysis revealed that all known orthologs of this protein are potential amyloids which possess several regions with conserved ability to aggregation. The biological role of nucleoporin amyloid formation is debatable. We suggest that it is a rather abnormal process, which is characteristic for many proteins implicated in phase separation.
AB - Amyloids are fibrillar protein aggregates with a cross-β structure and unusual features, including high resistance to detergent or protease treatment. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Several examples of nucleoporins (e.g., yeast Nup49, Nup100, Nup116, and human NUP153) are supposed to form amyloid fibrils. In this study, we demonstrated an ability of the human NUP58 nucleoporin to form amyloid aggregates in vivo and in vitro. Moreover, we found two forms of NUP58 aggregates: oligomers and polymers stabilized by disulfide bonds. Bioinformatic analysis revealed that all known orthologs of this protein are potential amyloids which possess several regions with conserved ability to aggregation. The biological role of nucleoporin amyloid formation is debatable. We suggest that it is a rather abnormal process, which is characteristic for many proteins implicated in phase separation.
KW - ArchCandy
KW - C-DAG
KW - Congo Red
KW - Evolution
KW - Human amyloids
KW - Nucleoporins
KW - Protein aggregation
KW - human amyloids
KW - BARRIER
KW - PRION
KW - evolution
KW - nucleoporins
KW - PREDICTION
KW - protein aggregation
KW - PROTEINS
KW - AGGREGATION
KW - NUCLEAR-PORES
KW - PLASTICITY
UR - https://www.mdpi.com/2227-9059/9/10/1451
UR - http://www.scopus.com/inward/record.url?scp=85118340244&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/8b416f87-f437-368e-b065-e41a79e9b161/
U2 - 10.3390/biomedicines9101451
DO - 10.3390/biomedicines9101451
M3 - Article
VL - 9
JO - Biomedicines
JF - Biomedicines
SN - 2227-9059
IS - 10
M1 - 1451
ER -
ID: 86420176