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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Vesicular Tubular Clusters

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.
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Golgi Apparatus01:09

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Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
Coat Assembly and GTPases01:33

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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.
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Regulated mRNA Transport

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Related Experiment Video

Updated: Jul 20, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
11:27

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

Subcellular localization of CIAPIN1.

Zhiming Hao1, Xiaohua Li, Taidong Qiao

  • 1State Key Laboratory of Cancer Biology, Institute of Digestive Diseases, Xijing Hospital, The Fourth Military Medical University, Xi'an 710032, Shaanxi Province, China.

The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society
|September 8, 2006
PubMed
Summary

Cytokine-induced apoptosis inhibitor 1 (CIAPIN1) is an anti-apoptotic molecule. This study reveals CIAPIN1 localizes to the cytoplasm, nucleus, and nucleolus, suggesting a translocation process.

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Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
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Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

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Last Updated: Jul 20, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
11:27

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Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ
09:34

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Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
11:06

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Published on: June 30, 2018

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Cytokine-induced apoptosis inhibitor 1 (CIAPIN1) is an identified anti-apoptotic molecule.
  • CIAPIN1 is expressed in human tissues and confers multidrug resistance in gastric cancer.
  • The fundamental biological functions of CIAPIN1 remain largely unelucidated.

Purpose of the Study:

  • To predict and characterize the subcellular localization of CIAPIN1.
  • To investigate the intracellular localization of CIAPIN1 in human and mouse cells.
  • To explore the potential translocation of CIAPIN1 within the cell.

Main Methods:

  • Bioinformatic prediction of subcellular localization.
  • Immunohistochemistry and immunofluorescence assays.
  • His-tagged CIAPIN1 expression and Western blotting analysis of subcellular fractions.

Main Results:

  • Consistent results across all methods indicated CIAPIN1 localization in the cytoplasm and nucleus.
  • CIAPIN1 was observed to accumulate specifically in the nucleolus.
  • Bioinformatic analysis identified putative nuclear localization and export signals in CIAPIN1.

Conclusions:

  • CIAPIN1 is localized in the cytoplasm, nucleus, and nucleolus.
  • The presence of signaling motifs suggests CIAPIN1 undergoes translocation.
  • CIAPIN1 may translocate between the cytoplasm, nucleus, and nucleolus, indicating a dynamic cellular role.