دورية أكاديمية

Nuclear import of histones.

التفاصيل البيبلوغرافية
العنوان: Nuclear import of histones.
المؤلفون: Bernardes NE; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A., Chook YM; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.
المصدر: Biochemical Society transactions [Biochem Soc Trans] 2020 Dec 18; Vol. 48 (6), pp. 2753-2767.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
اللغة: English
بيانات الدورية: Publisher: Portland Press On The Behalf Of The Biochemical Society Country of Publication: England NLM ID: 7506897 Publication Model: Print Cited Medium: Internet ISSN: 1470-8752 (Electronic) Linking ISSN: 03005127 NLM ISO Abbreviation: Biochem Soc Trans Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London : Portland Press On The Behalf Of The Biochemical Society
مواضيع طبية MeSH: Cell Nucleus/*metabolism , Cytoplasm/*metabolism , Histones/*metabolism , Karyopherins/*chemistry, Active Transport, Cell Nucleus ; Cell Cycle Proteins/metabolism ; GTP Phosphohydrolases/chemistry ; Histones/chemistry ; Humans ; Molecular Chaperones/metabolism ; Nuclear Proteins/metabolism ; Protein Conformation ; Protein Processing, Post-Translational ; Receptors, Cytoplasmic and Nuclear/metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/metabolism
مستخلص: The transport of histones from the cytoplasm to the nucleus of the cell, through the nuclear membrane, is a cellular process that regulates the supply of new histones in the nucleus and is key for DNA replication and transcription. Nuclear import of histones is mediated by proteins of the karyopherin family of nuclear transport receptors. Karyopherins recognize their cargos through linear motifs known as nuclear localization/export sequences or through folded domains in the cargos. Karyopherins interact with nucleoporins, proteins that form the nuclear pore complex, to promote the translocation of their cargos into the nucleus. When binding to histones, karyopherins not only function as nuclear import receptors but also as chaperones, protecting histones from non-specific interactions in the cytoplasm, in the nuclear pore and possibly in the nucleus. Studies have also suggested that karyopherins might participate in histones deposition into nucleosomes. In this review we describe structural and biochemical studies from the last two decades on how karyopherins recognize and transport the core histone proteins H3, H4, H2A and H2B and the linker histone H1 from the cytoplasm to the nucleus, which karyopherin is the major nuclear import receptor for each of these histones, the oligomeric state of histones during nuclear import and the roles of post-translational modifications, histone-chaperones and RanGTP in regulating these nuclear import pathways.
(© 2020 The Author(s).)
معلومات مُعتمدة: R01 GM069909 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: chromatin; histones; importins; karyopherins; nuclear pore complex; nuclear protein transport
المشرفين على المادة: 0 (Cell Cycle Proteins)
0 (Histones)
0 (Karyopherins)
0 (Molecular Chaperones)
0 (Nuclear Proteins)
0 (Receptors, Cytoplasmic and Nuclear)
0 (Saccharomyces cerevisiae Proteins)
EC 3.6.1.- (GTP Phosphohydrolases)
تواريخ الأحداث: Date Created: 20201210 Date Completed: 20210809 Latest Revision: 20210809
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC7752055
DOI: 10.1042/BST20200572
PMID: 33300986
قاعدة البيانات: MEDLINE
الوصف
تدمد:1470-8752
DOI:10.1042/BST20200572