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Crystal structure of progeria mutant S143F lamin A/C reveals increased hydrophobicity driving nuclear deformation
DC Field | Value | Language |
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dc.contributor.author | Ahn, Jinsook | - |
dc.contributor.author | Jeong, Soyeon | - |
dc.contributor.author | Kang, So-mi | - |
dc.contributor.author | Jo, Inseong | - |
dc.contributor.author | Park, Bum-Joon | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.date.accessioned | 2022-05-16T08:54:22Z | - |
dc.date.available | 2022-05-16T08:54:22Z | - |
dc.date.created | 2022-04-15 | - |
dc.date.created | 2022-04-15 | - |
dc.date.created | 2022-04-15 | - |
dc.date.created | 2022-04-15 | - |
dc.date.created | 2022-04-15 | - |
dc.date.issued | 2022-12 | - |
dc.identifier.citation | Communications Biology, Vol.5 No.1, p. 267 | - |
dc.identifier.issn | 2399-3642 | - |
dc.identifier.uri | https://hdl.handle.net/10371/179810 | - |
dc.description.abstract | Lamins are intermediate filaments that form a 3-D meshwork in the periphery of the nuclear envelope. The recent crystal structure of a long fragment of human lamin A/C visualized the tetrameric assembly unit of the central rod domain as a polymerization intermediate. A genetic mutation of S143F caused a phenotype characterized by both progeria and muscular dystrophy. In this study, we determined the crystal structure of the lamin A/C fragment harboring the S143F mutation. The obtained structure revealed the X-shaped interaction between the tetrameric units in the crystals, potentiated by the hydrophobic interactions of the mutated Phe143 residues. Subsequent studies indicated that the X-shaped interaction between the filaments plays a crucial role in disrupting the normal lamin meshwork. Our findings suggest the assembly mechanism of the 3-D meshwork and further provide a molecular framework for understanding the aging process by nuclear deformation. Increased hydrophobicity identified by the crystal structure presented in this work suggests a mechanism by which the S143F form of lamin A/C leads to progeria, a rapid aging syndrome. The authors observed aberrant molecular interactions that appear to lead to the nuclear deformation seen in other progeroid syndromes. | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Crystal structure of progeria mutant S143F lamin A/C reveals increased hydrophobicity driving nuclear deformation | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s42003-022-03212-3 | - |
dc.citation.journaltitle | Communications Biology | - |
dc.identifier.wosid | 000773289700001 | - |
dc.identifier.scopusid | 2-s2.0-85127293222 | - |
dc.citation.number | 1 | - |
dc.citation.startpage | 267 | - |
dc.citation.volume | 5 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Ha, Nam-Chul | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | INTERMEDIATE-FILAMENTS | - |
dc.subject.keywordPlus | ARCHITECTURE | - |
dc.subject.keywordPlus | CARDIOMYOPATHY | - |
dc.subject.keywordPlus | INSIGHTS | - |
dc.subject.keywordPlus | CELLS | - |
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