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関連する概念動画

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.7K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.7K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.4K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
3.4K
ER Retrieval Pathway01:45

ER Retrieval Pathway

5.0K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
5.0K
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.9K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.9K
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
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

5.7K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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関連する実験動画

Updated: Apr 3, 2026

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

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マイクロセファリー関連タンパク質YIPF5は,ERの輸出を差異的に調節する.

Francesca Bruno1, Mihaela Anitei1, Domenico Di Fraia1

  • 1Leibniz Institute on Aging, Fritz-Lipmann Institute, Beutenbergstr. 11, 07745 Jena, Germany.

iScience
|February 20, 2026
PubMed
まとめ
この要約は機械生成です。

YIPF5タンパク質は,神経細胞の発達に不可欠なER輸出を調節する. その障害は,タンパク質の輸送と細胞の移動に影響を与えることで,小頭症,,新生児糖尿病症候群 (MEDS2) を引き起こします.

キーワード:
細胞生物学 細胞生物学神経科学は神経科学である.

さらに関連する動画

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

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関連する実験動画

Last Updated: Apr 3, 2026

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

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科学分野:

  • 細胞生物学 細胞生物学
  • 神経科学は神経科学である.
  • 遺伝学 遺伝学とは

背景:

  • YIPF5は,ER-Golgi輸送に関与するエンドプラズマ網膜 (ER) の膜タンパク質です.
  • YIPF5の変異により,MEDS2が発症し,これは重度の幼児期障害である.
  • タンパク質の輸出におけるYIPF5の正確な役割と,神経学的欠陥との関連は完全に理解されていません.

研究 の 目的:

  • ERエクスポートにおけるYIPF5の機能と,神経学的発達への貢献を明らかにする.
  • YIPF5とERの輸出受容体SURF4.4の相互作用を調査する.
  • YIPF5に関連した発達障害の基礎となる分子機構を理解する.

主な方法:

  • YIPF5 ノックアウトおよび枯渇細胞モデル.
  • 細胞表面のタンパク質プロファイルとセクレトームの分析.
  • 傷を治すアッセイは,細胞の移住を評価する.
  • タンパク質の局所化を研究するための免疫光顕微鏡 (ERGIC53, Rab1).
  • ERの輸出の動態分析.
  • ネズミの胚の内臓内でのノックダウン.

主要な成果:

  • YIPF5はSURF4と直接相互作用し,SURF4貨物のER輸出を規制する.
  • YIPF5欠乏症は細胞表面タンパク質を変化させ,神経結合分子を減少させ,ERチャペロン分泌を増大させます.
  • YIPF5の枯渇は細胞の移動を促進し,SURF4の局所化を妨害し,異常なERチューブルを形成します.
  • 子宮内でのYipf5のノックダウンは,早すぎるニューロン移動とマウスの脳における形態学的欠陥を引き起こす.

結論:

  • YIPF5とSURF4は,重要なタンパク質のER輸出を調整するために協力しています.
  • YIPF5機能の障害は,皮質の発達障害の基礎であり,潜在的に小頭症を引き起こす可能性があります.
  • YIPF5は,神経細胞の移動と脳の発達を調節する上で重要な役割を果たします.