Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.4K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
7.4K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

11.0K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
11.0K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

8.1K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
8.1K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.9K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.9K
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

1.0K
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
1.0K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.6K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
19.6K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Joint Impact of Triglyceride-glucose Index and Free Fatty Acid Levels on Cardiovascular Outcomes in Overweight or Obese Patients with Coronary Artery Disease - A Large Multicenter Prospective Study.

Biomedical and environmental sciences : BES·2026
Same author

Systematic discovery of pathogen effector functions across human pathogens and pathways.

Cell·2026
Same author

Efficacy and Safety of Shen-Ling-Lian-Xia Granule Combined With Neoadjuvant Chemotherapy in Patients With Triple-Negative Breast Cancer: Protocol for a Randomized, Double-Blind, Multicenter Clinical Trial.

JMIR research protocols·2026
Same author

The Chinese Eating Disorder Brief Screening Scale (CEDBS): Development and Psychometric Validation in General and Clinical Populations.

The International journal of eating disorders·2026
Same author

Gender differences in relationships among parenting dimensions, disordered eating, and psychological factors in adolescents: a network analysis.

Journal of eating disorders·2026
Same author

Development and pilot evaluation of a culturally adapted CBT-based group intervention for body image dissatisfaction among at-risk Chinese college students.

Journal of eating disorders·2026

関連する実験動画

Updated: Apr 6, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.2K

ポリペプチド処理と分泌トランスポーターの結晶構造

David Yin-wei Lin1, Shuo Huang2, Jue Chen1

  • 11] Laboratory of Membrane Biology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA [2] Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.

Nature
|July 24, 2015
PubMed
まとめ

ペプチダースを含むATP結合カセットトランスポーター (PCAT) は単純な細菌のタンパク質分泌装置である. 結晶構造は,ATP結合がPCATを調節する方法を明らかにする.

科学分野:

  • 微生物学と分子生物学
  • タンパク質の分泌メカニズム
  • バクテリア細胞生物学

背景:

  • 細菌は分泌されるペプチドとタンパク質を コミュニケーション,競争,宿主操作のために利用する.
  • 細菌の膜に タンパク質が転移する過程は 多種多様な仕組みを伴う.
  • ペプチダースを含むATP結合カセットトランスポーター (PCAT) は,これらのシステムの構造的に単純なクラスです.

研究 の 目的:

  • タンパク質転位におけるPCATの構造的・機能的メカニズムを解明する.
  • PCATの活性と基板の処理におけるATP結合の役割を調査する.

主な方法:

  • クロストリジウム・サーモセルラムからPCAT1のX線結晶撮影
  • プロテアゼの活性と転位経路の機能を評価する生化学的測定法

主要な成果:

  • PCAT1の決定された結晶構造は,大きなα-ヘリクセル型トランスロケーション経路を明らかにする.
  • この経路は小さな折りたたまれたタンパク質を収納することが示された.
  • ATP結合は,経路へのアクセスとプロテアゼの活性を動的に制御し,基板の処理と輸出を結び付けます.

さらに関連する動画

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

15.6K

関連する実験動画

Last Updated: Apr 6, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.2K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

15.6K

結論:

  • PCATはATPに依存するメカニズムを使用して基質の成熟と転位を調整します.
  • 解明されたメカニズムは,細菌のタンパク質分泌と潜在的な治療標的の洞察を提供します.