دورية أكاديمية
أعرض في EDS

Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.

التفاصيل البيبلوغرافية
العنوان: Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.
المؤلفون: Nordeen SA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA., Turman DL; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA., Schwartz TU; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA. tus@mit.edu.
المصدر: Nature communications [Nat Commun] 2020 Nov 27; Vol. 11 (1), pp. 6060. Date of Electronic Publication: 2020 Nov 27.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Conserved Sequence*, Cell Membrane/*metabolism , Nuclear Pore Complex Proteins/*chemistry , Saccharomyces cerevisiae/*metabolism , Saccharomyces cerevisiae Proteins/*chemistry, Amino Acid Motifs ; Humans ; Models, Molecular ; Nuclear Pore Complex Proteins/metabolism ; Protein Domains ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Homology, Amino Acid
مستخلص: The hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential scaffolding component of the NPC. Here we report two nanobody-bound structures: the full-length Nup84-Nup133 C-terminal domain complex and the Nup133 N-terminal domain, both from S. cerevisiae. Together with previously published structures, this work enables the structural description of the entire 575 kDa Y complex from one species. The structure of Nup84-Nup133 CTD details the high flexibility of this dimeric unit of the Y complex. Further, the Nup133 NTD contains a structurally conserved amphipathic lipid packing sensor motif, confirmed by liposome interaction studies. The presented structures reveal important details about the function of the Y complex that affect our understanding of NPC structure and assembly.
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معلومات مُعتمدة: T32 GM007287 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (NUP133 protein, S cerevisiae)
0 (NUP84 protein, S cerevisiae)
0 (Nuclear Pore Complex Proteins)
0 (Saccharomyces cerevisiae Proteins)
تواريخ الأحداث: Date Created: 20201128 Date Completed: 20201209 Latest Revision: 20230106
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC7695694
DOI: 10.1038/s41467-020-19885-5
PMID: 33247142
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-020-19885-5