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@article{df64ba2e5bbf4237858d230844b9c2ab,
title = "The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo",
abstract = "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.",
keywords = "ArchCandy, C-DAG, Congo Red, Evolution, Human amyloids, Nucleoporins, Protein aggregation, human amyloids, BARRIER, PRION, evolution, nucleoporins, PREDICTION, protein aggregation, PROTEINS, AGGREGATION, NUCLEAR-PORES, PLASTICITY",
author = "Данилов, {Лаврентий Глебович} and Москаленко, {Светлана Евгеньевна} and Матвеенко, {Андрей Георгиевич} and Суханова, {Ксения Владимировна} and Белоусов, {Михаил Владимирович} and Журавлева, {Галина Анатольевна} and Бондарев, {Станислав Александрович}",
note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2021",
month = oct,
day = "13",
doi = "10.3390/biomedicines9101451",
language = "English",
volume = "9",
journal = "Biomedicines",
issn = "2227-9059",
publisher = "MDPI AG",
number = "10",

}

RIS

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