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SorCS3 does not require propeptide cleavage to bind nerve growth factor.

U B Westergaard¹, K Kirkegaard, E S Sørensen

¹Institute of Medical Biochemistry, Ole Worms Allé, bldg. 170, University of Aarhus, 8000 Aarhus C, Denmark.

|February 16, 2005

Summary

The Vps10p-domain receptor SorCS3 is processed in the Golgi and primarily located on the cell surface. This neurotrophin receptor is distinct from Sortilin and SorLA, with unique functional properties.

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Area of Science:

Cell biology
Neuroscience
Molecular biology

Background:

The Vps10p-domain receptor family plays crucial roles in protein trafficking and signaling.
Functional properties of SorCS3, a member of this family, remain largely uncharacterized.

Purpose of the Study:

To investigate the cellular processing, sorting, and ligand-binding properties of the SorCS3 receptor.
To elucidate the distinct functional characteristics of SorCS3 compared to related receptors like Sortilin and SorLA.

Main Methods:

Analysis of SorCS3 processing and maturation in cellular transfectants.
Biochemical assays to determine ligand binding to purified SorCS3.
Expression studies using wild-type and chimeric SorCS3 receptors.

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Main Results:

SorCS3 is synthesized as a proprotein, with N-terminal propeptide cleavage occurring in distal Golgi compartments.
The propeptide is not essential for SorCS3 maturation and does not impede ligand binding.
SorCS3 is predominantly localized to the plasma membrane, exhibits slow internalization, and limited intracellular trafficking.
SorCS3 binds neurotrophins and displays functional properties distinct from Sortilin and SorLA.

Conclusions:

SorCS3 undergoes specific post-translational modifications and exhibits unique cellular localization and trafficking patterns.
SorCS3 represents a novel neurotrophin receptor with a distinct functional profile within the Vps10p-domain receptor family.