Technology Report

Examining requirement for formation of functional Presenilin proteins and their processing events in vivo

  1. Ala Barakat1,
  2. Bettie Mercer1,
  3. Emilie Cooper1,2,
  4. Hui-Min Chung1,*

Article first published online: 3 FEB 2009

DOI: 10.1002/dvg.20475

Issue

genesis

genesis

Volume 47, Issue 3, pages 161–168, March 2009

Additional Information

How to Cite

Barakat, A., Mercer, B., Cooper, E. and Chung, H.-M. (2009), Examining requirement for formation of functional Presenilin proteins and their processing events in vivo. Genesis, 47: 161–168. doi: 10.1002/dvg.20475

Author Information

  1. 1

    Department of Biology, University of West Florida, Pensacola, Florida

  2. 2

    Environmental Protection Agency, Gulf Ecology Division, Gulf Breeze, Florida

*Department of Biology, University of West Florida, 11000 University Parkway, Pensacola, FL

Publication History

  1. Issue published online: 23 MAR 2009
  2. Article first published online: 3 FEB 2009
  3. Manuscript Accepted: 21 OCT 2008
  4. Manuscript Revised: 19 OCT 2008
  5. Manuscript Received: 8 SEP 2008

Funded by

  • NIH. Grant Number: 1R15AG028448-01
  • University of West Florida

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Keywords:

  • Presenilin;
  • γ-secretase;
  • Presenilinase-mediated endoproteolysis;
  • Notch;
  • Drosophila

Abstract

Presenilin (Psn) is a multipass transmembrane protein that functions as the catalytic subunit of γ-secretase for mediating intramembrane cleavage of type 1 transmembrane proteins. Normally active Psn is in the form of a heterodimer composed by its N-terminal and C-terminal fragments that are generated from a Presenilinase-mediated endoproteolytic cleavage within its large cytosolic loop during assembly of the protease complex. Using the Psn forms that either bypass or disable Presenilinase-mediated endoproteolysis, and a Psn form that has most of the large cytosolic loop deleted, we have established an in vivo system to enable investigations of Psn functional domains in Drosophila. We show that the Presenilinase-mediated endoproteolytic event is not essential for producing Psn activity during animal development, and is regulated by integrity of the large cytosolic loop of Psn in Drosophila. The Psn transgenic flies described here could be applied to a broad range of studies on Psn functioning and its related γ-secretase activity at any developmental stage. genesis 47:161–168, 2009. © 2009 Wiley-Liss, Inc.

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