Macromolecular complexes as depots for releasable regulatory proteins.
Partho Sarothi Ray1, Abul Arif, Paul L Fox
1Department of Cell Biology, Lerner Research Institute, Cleveland Clinic, 9500 Euclid Avenue/NC10, Cleveland, OH 44195, USA.
Trends in Biochemical Sciences
|February 27, 2007
Summary
Multi-component cellular complexes act as depots, storing regulatory proteins. Upon release, these proteins gain new functions, influencing cellular processes like inflammation and translation.
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- Multi-component macromolecular complexes are vital for cellular functions, coordinating activities and regulating protein levels.
- These complexes ensure the spatial and temporal organization of cellular processes.
Purpose of the Study:
- To propose a novel function of multi-component complexes as depots for regulatory proteins.
- To investigate the inducible and context-dependent release of these proteins for auxiliary functions.
- To examine the ribosome and tRNA multi-synthetase complex as examples of such depots.
Main Methods:
- Analysis of existing literature and experimental data on the ribosome and tRNA multi-synthetase complex.
- Comparative analysis of protein release mechanisms in different cellular assemblies.
Main Results:
- The ribosome and tRNA multi-synthetase complex serve dual roles: protein synthesis and regulatory protein depots.
- Released proteins from these complexes are involved in inflammation-responsive, transcript-specific translational control.
- Evidence suggests this depot mechanism may be widespread in biological systems.
Conclusions:
- Multi-component complexes can function as inducible depots for regulatory proteins.
- Released proteins acquire auxiliary functions, impacting cellular regulation.
- The depot mechanism represents a potentially widespread strategy in nature for protein regulation.
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