Book chapter
Analysis of Dimerization Determinants of PDE6 Catalytic Subunits
Phosphodiesterase Methods and Protocols, pp.263-275
Methods In Molecular Biology, 307, Humana Press
2005
DOI: 10.1385/1-59259-839-0:263
PMID: 15988069
Abstract
An absolute majority of cyclic nucleotide phosphodiesterases (PDEs) form catalytic dimers. The structural determinants and functional significance of PDE dimerization are poorly understood. Furthermore, all known dimeric PDEs with the exception of retinal rod guanosine 3′,5′-cyclic-monophosphate PDE (PDE6) are homodimeric enzymes. Rod PDE6 is a catalytic heterodimer composed of α- and β-subunits. Gel filtration, sucrose gradient centrifugation, and immunoprecipitation are standard techniques used to study dimerization of proteins. We successfully applied these methods to investigate dimerization of chimeric proteins between PDE6αβ and PDE5, which allowed us to elucidate the structural basis for heterodimerization of rod PDE6. This chapter outlines approaches to the investigation of PDE6 dimerization that can be utilized in a broader analysis of PDE dimerization.
Details
- Title: Subtitle
- Analysis of Dimerization Determinants of PDE6 Catalytic Subunits
- Creators
- Khakim G Muradov - Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa CityKimberly K Boyd - Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa CityNikolai O Artemyev - Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City
- Resource Type
- Book chapter
- Publication Details
- Phosphodiesterase Methods and Protocols, pp.263-275
- Publisher
- Humana Press; Totowa, NJ
- Series
- Methods In Molecular Biology; 307
- DOI
- 10.1385/1-59259-839-0:263
- PMID
- 15988069
- eISSN
- 1940-6029
- ISSN
- 1064-3745
- Language
- English
- Date published
- 2005
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
- Record Identifier
- 9984070016202771
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