Secretion of endothelin converting enzyme-1a: The hydrophobic signal anchor domain alone is not sufficient to promote membrane localization

S. Courtnie Brooks, Lizette Fernandez, Adviye Ergul

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Endothelin converting enzyme-1 (ECE-1) is a type II membrane protein that is important for the proteolytic activation of big endothelin-1 to endothelin-1. Although the highly conserved zinc-binding motif is known to be located in the extracellular domain, the role(s) 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, remain undetermined. In this study, we provide evidence that the deletion of the cytoplasmic N-terminal tail (residues 1-55) of ECE-1a results in the cleavage of a potential signal peptide located in the signal anchor domain leading to the partial secretion of the recombinant enzyme into the media. However, the truncation of N- terminal and/or signal anchor domain does not affect the activity of ECE-1a. Therefore, our results demonstrate 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)
Pages (from-to)45-51
Number of pages7
JournalMolecular and Cellular Biochemistry
Volume208
Issue number1-2
StatePublished - Jul 24 2000

Keywords

  • Endothelin converting enzyme
  • Membrane protein
  • Signal anchor domain

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Secretion of endothelin converting enzyme-1a: The hydrophobic signal anchor domain alone is not sufficient to promote membrane localization'. Together they form a unique fingerprint.

  • Cite this