دورية أكاديمية
أعرض في EDS

Mechanical stress-induced subcellular re-localization of N-terminally truncated tobacco Nt-4/1 protein.

التفاصيل البيبلوغرافية
العنوان: Mechanical stress-induced subcellular re-localization of N-terminally truncated tobacco Nt-4/1 protein.
المؤلفون: Atabekova AK; Department of Virology, Biological Faculty, Moscow State University, Moscow 119234, Russia., Lazareva EA; Department of Virology, Biological Faculty, Moscow State University, Moscow 119234, Russia., Strelkova OS; Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia., Solovyev AG; Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia; Sechenov First Moscow State Medical University, Institute of Molecular Medicine, Moscow 119991, Russia., Morozov SY; Department of Virology, Biological Faculty, Moscow State University, Moscow 119234, Russia; Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. Electronic address: morozov@genebee.msu.su.
المصدر: Biochimie [Biochimie] 2018 Jan; Vol. 144, pp. 98-107. Date of Electronic Publication: 2017 Oct 31.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Editions Scientifiques Elsevier Country of Publication: France NLM ID: 1264604 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1638-6183 (Electronic) Linking ISSN: 03009084 NLM ISO Abbreviation: Biochimie Subsets: MEDLINE
أسماء مطبوعة: Publication: Paris : Editions Scientifiques Elsevier
Original Publication: Paris.
مواضيع طبية MeSH: Sequence Deletion* , Stress, Mechanical* , Nicotiana*, Intracellular Space/*metabolism , Plant Proteins/*metabolism, Amino Acid Sequence ; Microtubules/metabolism ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Protein Transport
مستخلص: The Nicotiana tabacum 4/1 protein (Nt-4/1) of unknown function expressed in plant vasculature has been shown to localize to cytoplasmic bodies associated with endoplasmic reticulum. Here, we analyzed molecular interactions of an Nt-4/1 mutant with a deletion of 90 N-terminal amino acid residues (Nt-4/1d90) having a diffuse GFP-like localization. Upon transient co-expression with VAP27, a membrane protein known to localize to the ER, ER-plasma membrane contact sites and plasmodesmata, Nt-4/1d90 was concentrated around the cortical ER tubules, forming a network matching the shape of the cortical ER. Additionally, in response to mechanical stress, Nt-4/1d90 was re-localized to small spherical bodies, whereas the subcellular localization of VAP27 remained essentially unaffected. The Nt-4/1d90-containing bodies associated with microtubules, which underwent noticeable bundling under the conditions of mechanical stress. The Nt-4/1d90 re-localization to spherical bodies could also be induced by incubation at an elevated temperature, although under heat shock conditions the re-localization was less efficient and incomplete. An Nt-4/1d90 mutant, which had phosphorylation-mimicking mutations in a predicted cluster of four potentially phosphorylated residues, was found to both inefficiently re-localize to spherical bodies and tend to revert back to the initial diffuse localization. The presented data show that Nt-4/1 has a potential for response to stresses that is manifested by its deletion mutant Nt-4/1d90, and this response can be mediated by protein dephosphorylation.
(Copyright © 2017 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)
فهرسة مساهمة: Keywords: Endoplasmic reticulum; Mechanical stress; Plant protein; Protein phosphorylation; Subcellular localization
المشرفين على المادة: 0 (Plant Proteins)
تواريخ الأحداث: Date Created: 20171104 Date Completed: 20180724 Latest Revision: 20231213
رمز التحديث: 20231215
DOI: 10.1016/j.biochi.2017.10.020
PMID: 29097279
قاعدة البيانات: MEDLINE
الوصف
تدمد:1638-6183
DOI:10.1016/j.biochi.2017.10.020