Expression and characterization of human PDEdelta and its Caenorhabditis elegans ortholog CEdelta.

Abstract

Cyclic GMP phosphodiesterase (PDE) is rod photoreceptor disk membrane-associated via C-terminal lipid tails. PDEdelta, a recently identified subunit, was shown to disrupt PDE/membrane interaction under physiological conditions, without affecting PDE catalytic activity. We found that a PDEdelta ortholog from the eyeless nematode Caenorhabditis elegans (termed CEdelta) solubilizes bovine PDE in vitro with an EC50 very similar to PDEdelta. Immobilized PDEdelta and CEdelta both bind, in addition to bovine PDE, an N-terminal fragment of human retinitis pigmentosa GTPase regulator, but not rhodopsin kinase and Ran binding protein 1. The results suggest that PDEdelta and CEdelta may regulate membrane binding of a variety of proteins in photoreceptors and other tissues.

• Authors: N Li, W Baehr
• Journal: FEBS letters (FEBS Lett) Vol. 440 Issue 3 Pg. 454-7 (Dec 04 1998) ISSN: 0014-5793 [Print] England
• PMID: 9872421 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Eye Proteins
• Helminth Proteins
• Recombinant Proteins
• Glutathione Transferase
• Phosphoric Diester Hydrolases
• 3',5'-Cyclic-GMP Phosphodiesterases
• Cyclic Nucleotide Phosphodiesterases, Type 6
• PDE6B protein, human

Topics

• 3',5'-Cyclic-GMP Phosphodiesterases (biosynthesis, genetics, metabolism)
• Animals
• Caenorhabditis elegans (genetics, metabolism)
• Cattle
• Cell Membrane (metabolism)
• Cyclic Nucleotide Phosphodiesterases, Type 6
• Eye Proteins (biosynthesis, genetics, metabolism)
• Glutathione Transferase (metabolism)
• Helminth Proteins (biosynthesis, genetics, metabolism)
• Humans
• Phosphoric Diester Hydrolases (metabolism)
• Protein Binding
• Protein Folding
• Recombinant Proteins (biosynthesis, metabolism)
• Solubility