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The GxxxG motif in the transmembrane domain of AbetaPP plays an essential role in the interaction of CTF beta with the gamma-secretase complex and the formation of amyloid-beta
Journal of Alzheimer's disease : JAD (2009)
  • Guozhang Mao, University of Tennessee - Knoxville
  • Jianxin Tan, University of Tennessee - Knoxville
  • Mei-Zhen Cui, University of Tennessee - Knoxville
  • Dehua Chui
  • Xuemin Xu, University of Tennessee - Knoxville
Abstract
Gamma-secretase-mediated processing of the amyloid-beta protein precursor (AbetaPP) is a crucial step in the formation of the amyloid-beta peptide (Abeta), but little is known about how the substrate AbetaPP interacts with the gamma-secretase complex. To understand the molecular events involved in gamma-secretase-mediated AbetaPP processing and Abeta formation, in the present study we determined the role of a well conserved GxxxG motif in the transmembrane domain of AbetaPP. Our data clearly demonstrate that substitution of aspartic acid for the key glycine residues in the GxxxG motif almost completely abolished the formation of Abeta. Furthermore, our data revealed that substitution of aspartic acid for the glycine in this GxxxG motif disrupts the interaction of AbetaPP with the gamma-secretase complex. Thus, the present study revealed an essential role for the GxxxG motif in the interaction of AbetaPP with the gamma-secretase complex and the formation of Abeta.
Publication Date
2009
Citation Information
Guozhang Mao, Jianxin Tan, Mei-Zhen Cui, Dehua Chui, et al.. "The GxxxG motif in the transmembrane domain of AbetaPP plays an essential role in the interaction of CTF beta with the gamma-secretase complex and the formation of amyloid-beta" Journal of Alzheimer's disease : JAD Vol. 18 Iss. 1 (2009)
Available at: http://works.bepress.com/xuemin_xu/3/