Role of the hydrophobic transmembrane domain in membrane anchoring of endothelin-converting enzyme-1a

S. C. Brooks, A. Ergul

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Endothelin-converting enzyme-1 (ECE-1) is a type II membrane protein that cleaves big endothelin-1 (big ET-1) to endothelin-1 (ET-1). The role of the N-terminal and membrane-spanning signal anchor domains in the biosynthesis and function of ECE-1 isoforms, ECE-1a, ECE-1b and ECE-1c, remains unknown. This study provides evidence that the deletion of the cytoplasmic N-terminal tail (residues 1-55) of bovine ECE-1a results in the processing of a putative signal peptide located in the signal anchor domain leading to the partial secretion of the recombinant enzyme into the media. The truncation of N-terminal and/or signal anchor domain does not affect the activity of ECE-1a. These results indicate that the hydrophobic signal anchor domain alone is not sufficient for the membrane anchoring of ECE-1a and that the N-terminal domain of ECE-1a is important for membrane targeting as well as the intracellular localization of the enzyme.

Original languageEnglish (US)
JournalJournal of Cardiovascular Pharmacology
Volume36
Issue number5 SUPPL. 1
DOIs
StatePublished - Jan 1 2000
Externally publishedYes

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Endothelin-1
Membranes
Enzymes
Protein Sorting Signals
Protein Isoforms
Membrane Proteins
Endothelin-Converting Enzymes

Keywords

  • Endothelin-converting enzyme (ECE)
  • Membrane protein
  • Signal anchor domain

ASJC Scopus subject areas

  • Pharmacology
  • Cardiology and Cardiovascular Medicine

Cite this

Role of the hydrophobic transmembrane domain in membrane anchoring of endothelin-converting enzyme-1a. / Brooks, S. C.; Ergul, A.

In: Journal of Cardiovascular Pharmacology, Vol. 36, No. 5 SUPPL. 1, 01.01.2000.

Research output: Contribution to journalArticle

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N2 - Endothelin-converting enzyme-1 (ECE-1) is a type II membrane protein that cleaves big endothelin-1 (big ET-1) to endothelin-1 (ET-1). The role of the N-terminal and membrane-spanning signal anchor domains in the biosynthesis and function of ECE-1 isoforms, ECE-1a, ECE-1b and ECE-1c, remains unknown. This study provides evidence that the deletion of the cytoplasmic N-terminal tail (residues 1-55) of bovine ECE-1a results in the processing of a putative signal peptide located in the signal anchor domain leading to the partial secretion of the recombinant enzyme into the media. The truncation of N-terminal and/or signal anchor domain does not affect the activity of ECE-1a. These results indicate that the hydrophobic signal anchor domain alone is not sufficient for the membrane anchoring of ECE-1a and that the N-terminal domain of ECE-1a is important for membrane targeting as well as the intracellular localization of the enzyme.

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