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Updated: May 19, 2026
13:08
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Cargo carriers from the Golgi to the cell surface
1Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA. pfeffer@stanford.edu
The EMBO Journal
|September 4, 2012
Summary
Researchers discovered a new class of secretory carriers, termed CARTS (cargo carriers), which transport smaller molecules. These carriers utilize myosin for movement but not for their assembly.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Secretory pathways are crucial for protein and cargo transport within cells.
- Understanding the diversity of secretory carriers is essential for cellular function.
Purpose of the Study:
- To identify and characterize novel secretory cargo carriers.
- To elucidate the molecular mechanisms governing the formation and motility of these carriers.
Main Methods:
- Biochemical approaches were employed to isolate and analyze secretory carriers.
- Characterization involved assessing the cargo content and identifying key proteins involved in carrier formation and movement.
Main Results:
- A new class of secretory cargo carriers (CARTS) was identified.
- CARTS do not contain large cargoes like collagen or VSV-G glycoprotein.
- These carriers are directed towards the basolateral membrane and use myosin for motility, but not formation.
Conclusions:
- CARTS represent a distinct class of secretory vesicles.
- Myosin plays a role in the motility of CARTS, independent of their formation process.
- This discovery expands our understanding of the cellular secretory machinery.
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