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RanBP9 controls the oligomeric state of CTLH complex assemblies
Pia Maria van Gen Hassend1, Aparna Pottikkadavath1, Carolyn Delto1
1Julius-Maximilians-Universität Würzburg, Rudolf Virchow Center for Integrative and Translational Bioimaging, Institute of Structural Biology, Würzburg, Germany.
The Journal of Biological Chemistry
|January 9, 2023
Summary
The C-terminal to lissencephaly-1 homology motif (CTLH) complex
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- The C-terminal to lissencephaly-1 homology motif (CTLH) complex is a multisubunit RING E3 ligase.
- Its substrate specificity and subunit composition are not well-defined.
- Two key subunits, muskelin and Wdr26, define alternative CTLH complexes with distinct quaternary structures.
Purpose of the Study:
- To characterize the assembly pathways of the CTLH complex.
- To elucidate the role of specific subunits (muskelin, Wdr26, RanBP9, Twa1, Armc8β) in CTLH complex architecture.
- To understand how alternative assembly pathways are governed.
Main Methods:
- Biophysical techniques
- Biochemical techniques
- Analysis of subunit interactions and oligomerization
Main Results:
- Muskelin tetramerization and Wdr26 dimerization form mutually exclusive oligomerization modules.
- These modules compete for RanBP9 binding with nanomolar affinity.
- Armc8β and Twa1 form a heterodimer and interact with RanBP9.
- RanBP9 organizes subunit assembly and prevents higher-order oligomerization.
Conclusions:
- Alternative assembly pathways for the CTLH complex exist.
- RanBP9 plays a critical role in governing differential oligomeric assemblies.
- This work advances mechanistic understanding of CTLH complex architectures.
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