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How many lives does CLIMP-63 have?
Patrick A Sandoz1, F Gisou van der Goot1
1*Global Health Institute, Ecole Polytechnique Fédérale de Lausanne, Station 19, 1015 Lausanne, Switzerland.
Biochemical Society Transactions
|April 8, 2015
Summary
This review covers 20 years of research on cytoskeleton-linking membrane protein 63 (CLIMP-63). CLIMP-63 is a transmembrane protein involved in endoplasmic reticulum structure and cell surface receptor functions.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- CLIMP-63 (cytoskeleton-linking membrane protein 63), also known as CKAP4, was first reviewed in 1995.
- This review focuses on the subsequent 20 years of research into this enigmatic protein.
Purpose of the Study:
- To synthesize current knowledge on CLIMP-63's structure and functions.
- To discuss the protein's roles in the endoplasmic reticulum and at the cell surface.
- To highlight gaps in understanding regarding its functions and post-translational modifications.
Main Methods:
- Literature review of research published over 20 years.
- Analysis of studies investigating CLIMP-63's molecular interactions and cellular localization.
- Synthesis of findings on CLIMP-63's biophysical and biochemical properties.
Main Results:
- CLIMP-63 is a type II transmembrane protein.
- Its cytosolic domain binds microtubules, while the luminal domain forms homo-oligomers, stabilizing endoplasmic reticulum sheets.
- CLIMP-63 functions as a ligand-activated receptor at the cell surface.
Conclusions:
- CLIMP-63 possesses dual localization and function within the cell.
- Further research is needed to elucidate the precise mechanisms and regulation of its diverse roles.
- Post-translational modifications likely play a critical role in controlling CLIMP-63 activity.
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