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Related Concept Videos

Golgi Apparatus

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.

Golgi Apparatus

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 Apparatus

Golgi Apparatus

Golgi Matrix Proteins

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...

Vesicular Tubular Clusters

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.
With the help of motor proteins such...

Transport Across the Golgi

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...

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Related Experiment Video

Updated: Apr 19, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

mTORC1 gRABs the Golgi.

Joan Sanchez-Gurmaches¹, David A Guertin¹

¹Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.

|December 18, 2014

Summary

This summary is machine-generated.

A novel Golgi-based pathway for sensing amino acids by mTORC1, independent of Rag GTPases, has been discovered. This Rab1A GTPase mechanism in colorectal cancer links to mTORC1 activity and drug sensitivity.

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Published on: October 20, 2023

Area of Science:

Cellular Biology
Molecular Oncology
Signal Transduction

Background:

The mechanistic target of rapamycin complex 1 (mTORC1) is a central regulator of cell growth and metabolism.
Rag GTPases mediate lysosome-based amino acid sensing to control mTORC1.
Alternative nutrient-sensing mechanisms for mTORC1 remain incompletely understood.

Purpose of the Study:

To investigate a potential alternative pathway for amino acid sensing by mTORC1.
To explore the role of Rab1A GTPase in mTORC1 regulation.
To assess the relevance of this pathway in colorectal cancer.

Main Methods:

Biochemical assays to study mTORC1 localization and activity.
Genetic manipulation of Rab1A and Rag GTPases.
Analysis of colorectal cancer patient samples.

Main Results:

A novel Golgi-based mechanism for amino acid sensing by mTORC1, independent of Rag GTPases, was identified.
The Rab1A GTPase mediates this Golgi-centric sensing pathway.
Rab1A overexpression in colorectal cancers correlates with increased mTORC1 activity and sensitivity to mTOR inhibitors.

Conclusions:

This study reveals a new paradigm for nutrient sensing by mTORC1, highlighting the Golgi apparatus as a key signaling hub.
Rab1A is a critical mediator of this alternative mTORC1 regulation.
The Rab1A-mTORC1 axis represents a potential therapeutic target in colorectal cancer.