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Related Concept Videos

Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...

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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Published on: August 10, 2017

Secretion without Golgi.

Igor Prudovsky1, Francesca Tarantini, Matteo Landriscina

  • 1Maine Medical Center Research Institute, Maine Medical Center, Scarborough, Maine 04074, USA. prudoi@mmc.org

Journal of Cellular Biochemistry
|September 6, 2007
PubMed
Summary

Certain proteins, like FGF1 and IL1alpha, exit cells via non-classical pathways. This stress-induced release involves membrane interactions and multiprotein complexes, offering therapeutic targets for various diseases.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteins lacking signal peptides are increasingly found to be secreted via non-classical pathways, bypassing the endoplasmic reticulum and Golgi.
  • Potent proangiogenic cytokines, Fibroblast Growth Factor 1 (FGF1) and Interleukin-1 alpha (IL1alpha), are among these non-classically secreted proteins.

Purpose of the Study:

  • To investigate the mechanisms of non-classical protein release, focusing on FGF1 and IL1alpha.
  • To identify the cellular components and processes involved in the stress-induced translocation of these proteins across the cell membrane.

Main Methods:

  • Analysis of protein interactions with cell membranes under stress conditions.
  • Investigation of copper-dependent multiprotein complex assembly during protein export.
  • Examination of the role of acidic phospholipids in membrane destabilization and protein release.

Main Results:

  • Stress-induced release of FGF1 and IL1alpha requires the formation of copper-dependent multiprotein complexes.
  • The process involves the interaction of these proteins with acidic phospholipids in the inner leaflet of the cell membrane, leading to membrane destabilization.
  • Thrombin treatment and Notch signaling inhibition also stimulate FGF1 export.

Conclusions:

  • Non-classical secretion of FGF1 and IL1alpha is a distinct cellular process regulated by specific molecular machinery.
  • The mechanisms elucidated provide a basis for targeting these pathways.
  • Non-classical release of FGF1 and IL1alpha represents a promising therapeutic strategy for cardiovascular, oncologic, and inflammatory diseases.