Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

The cleaved N-terminal signal sequence of the cardiac Na+-Ca2+ exchanger is not required for functional membrane integration

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Sahintoth, M.
  • Nicoll, D. A.
  • Frank, J. S.
  • Philipson, K. D.
  • Friedlander, Martin

publication date

  • 1995

journal

  • Biochemical and Biophysical Research Communications  Journal

abstract

  • The cardiac Na(+)-Ca2+ exchanger differs from most other polytopic membrane proteins in that the amino terminus is cleaved during integration into the endoplasmic reticulum membrane. In this study, the cleaved N-terminal signal sequence of the exchanger was deleted (DelSS) or rendered uncleavable by mutation of the cleavage site (MutSS). Functional analysis of the mutants expressed in Xenopus laevis oocytes and sf9 insect cells demonstrates that DelSS exchanger catalyzes Na(+)-dependent Ca2+ transport at wild-type levels, while activity of MutSS exchanger is reduced to approximately 60% of wild-type in oocytes and 20% in sf9 cells. These results indicate that neither the presence nor the cleavage of the signal peptide is required for functional assembly of the exchanger protein in the membrane. Furthermore, these observations support the concept that internal topogenic signals play the major role in membrane insertion of the Na(+)-Ca2+ exchanger.

subject areas

  • Animals
  • Base Sequence
  • Carrier Proteins
  • Cell Line
  • Cloning, Molecular
  • DNA Primers
  • Dogs
  • Endoplasmic Reticulum
  • Female
  • In Vitro Techniques
  • Intracellular Membranes
  • Molecular Sequence Data
  • Mutagenesis
  • Myocardium
  • Oocytes
  • Protein Biosynthesis
  • Protein Sorting Signals
  • Sodium-Calcium Exchanger
  • Spodoptera
  • Xenopus laevis
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1995.2064

PubMed ID

  • 7626138
scroll to property group menus

Additional Document Info

start page

  • 968

end page

  • 974

volume

  • 212

issue

  • 3

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support