Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.1K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
Protein Modifications in the RER01:26

Protein Modifications in the RER

6.8K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.8K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.0K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.6K
The Unfolded Protein Response01:37

The Unfolded Protein Response

6.2K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.2K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Ubiquitin beyond the proteome: lipids, glycans, metabolites, nucleic acids, and an expanding molecular landscape.

Biochemical Society transactions·2026
Same author

DAXX promotes SUMOylation of chromatin-trapped DNMT1.

Journal of biochemistry·2026
Same author

Pentosidine modification of neuronal proteins induces dendritic spine enlargement in vitro.

Biochemical and biophysical research communications·2025
Same author

Author Correction: Structures of α-synuclein filaments from multiple system atrophy.

Nature·2025
Same author

Ubiquitination-activated TAB-TAK1-IKK-NF-κB axis modulates gene expression for cell survival in the lysosomal damage response.

eLife·2025
Same author

Combinatorial ubiquitin code degrades deubiquitylation-protected substrates.

Nature communications·2025

相关实验视频

Updated: Jan 7, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

8.6K

NFE2L1/Nrf1形成一个联合激活器复杂的后:N-糖酶介导的序列编辑,并减轻蛋白质体功能障碍.

Yukiko Yoshida1, Meari Okada1, Naoko Arai1

  • 1Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|December 30, 2025
PubMed
概括

核因子红色素-2-样1 (Nrf1) 是通过序列编辑激活的,这是转录因子的独特过程. 这种编辑对于蛋白酶基因表达和细胞存活至关重要,但其构成性激活可能是有毒的.

关键词:
在 HCFC1 中,在 NFE2L1L1 中.NGLY1 是一个很好的标准.第1章 没有了蛋白质酶体蛋白质组是什么

更多相关视频

CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.
07:46

CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.

Published on: December 11, 2020

6.4K

相关实验视频

Last Updated: Jan 7, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

8.6K
CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.
07:46

CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.

Published on: December 11, 2020

6.4K

科学领域:

  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学
  • 生物化学 生物化学

背景情况:

  • 核因子红色素2样1 (NFE2L1/Nrf1) 是一种与ER相关的转录因子,调节蛋白质组基因.
  • Nrf1是独一无二的,因为它经历了对转录激活的序列编辑,这个过程涉及:N-糖酶 (NGLY1).

研究的目的:

  • 阐明序列编辑调节 Nrf1 的转录活动的机制.
  • 调查N-糖化位编辑在Nrf1的功能和细胞反应中的作用.

主要方法:

  • 在HeLa细胞中研究了人类Nrf1中N-糖化位的序列编辑.
  • 研究了Nrf1.1的蛋白相互作用和染色素结合.
  • 分析了Nrf1突变对细胞生长的影响.

主要成果:

  • 对 Nrf1 的 Asn574 位点进行序列编辑对于蛋白质酶基因表达和与宿主细胞因子 C1 和 O-GlcNAc 转移酶的相互作用至关重要.
  • 编辑其他N-糖基化位点有助于共同激活剂CREBBP/EP300的相互作用,增强转录活性.
  • 通过模仿蛋白质分解处理或NGLY1编辑Nrf1的构成性激活减少了细胞生长,表明了细胞毒性.

结论:

  • Nrf1激活是一种受调节的,按需的过程,在蛋白质体应激期间对细胞存活至关重要.
  • Nrf1的序列编辑是控制其转录活性和与协活性剂复合体相互作用的关键调节机制.
  • 不受控制的Nrf1激活会导致细胞毒性,这凸显了其调节表达的重要性.