Related Experiment Video
Updated: May 15, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Multiple TSC22D4 iso-/phospho-glycoforms display idiosyncratic subcellular localizations and interacting protein
Sonia Canterini1, Valentina Carletti, Stefania Nusca
1Department of Psychology, Pasteur Institute-Cenci Bolognetti Foundation and Daniel Bovet Neurobiology Research Center, Sapienza University of Rome, Rome, Italy.
TSC22D4 protein forms exhibit distinct subcellular localizations and interact with different partners during neuronal differentiation, revealing form-specific functions in cell processes like proliferation and apoptosis.
Area of Science:
- Molecular Biology
- Cell Biology
- Neuroscience
Background:
- TSC22D proteins, including TSC22D1 and TSC22D4, are crucial for cell proliferation, differentiation, and apoptosis.
- Their interaction mechanisms and functional roles remain largely uncharacterized.
Purpose of the Study:
- To biochemically characterize different TSC22D4 forms.
- To determine their subcellular localization and protein interactions during cerebellar granule neuron (CGN) differentiation.
Main Methods:
- Biochemical characterization of TSC22D4 splice variants (42 and 55 kDa) and post-translationally modified forms (67 and 72 kDa).
- Analysis of subcellular localization and protein partners in undifferentiated and differentiated CGNs.
Main Results:
- TSC22D4-42 localizes to the cytosol and interacts with TSC22D1.2 in undifferentiated CGNs.
- TSC22D4-55 associates with the nuclear matrix in differentiated CGNs.
- TSC22D4-67 localizes to cytosol, nuclei, and mitochondria, interacting with apoptosis factors.
- TSC22D4-72, O-GlcNAcylated and phosphorylated, binds to chromatin.
Conclusions:
- Different TSC22D4 forms display unique subcellular distributions and interaction profiles during CGN differentiation.
- These findings suggest form-specific functions for TSC22D proteins and offer a framework for further research.
More Related Videos
Related Concept Videos
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Vesicular Tubular Clusters
With the help of motor proteins such...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Golgi Matrix Proteins
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...

