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Pellegrini L, Passer BJ, Canelles M, et al. PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. J Alzheimers Dis. 2001;3(2):181-190doi: 10.3233/jad-2001-3203.
Pellegrini, L., Passer, B. J., Canelles, M., Lefterov, I., Ganjei, J. K., Fowlkes, B. J., Koonin, E. V., & D'Adamio, L. (2001). PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. Journal of Alzheimer's disease : JAD, 3(2), 181-190. https://doi.org/10.3233/jad-2001-3203
Pellegrini, Luca, et al. "PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2." Journal of Alzheimer's disease : JAD vol. 3,2 (2001): 181-190. doi: https://doi.org/10.3233/jad-2001-3203
Pellegrini L, Passer BJ, Canelles M, Lefterov I, Ganjei JK, Fowlkes BJ, Koonin EV, D'Adamio L. PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. J Alzheimers Dis. 2001 Apr;3(2):181-190. doi: 10.3233/jad-2001-3203. PMID: 12214059.
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J Alzheimers Dis. 2001 Apr;3(2):181-190. doi: 10.3233/jad-2001-3203.

PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2.

Journal of Alzheimer's disease : JAD

Luca Pellegrini, Brent J. Passer, Matilde Canelles, Ilyia Lefterov, J. Kelly Ganjei, B.J. Fowlkes, Eugene V. Koonin, Luciano D'Adamio

Affiliations

  1. Laboratory of Cellular and Molecular Immunology, NIH, Bethesda, MD, 20892, USA.

PMID: 12214059 DOI: 10.3233/jad-2001-3203

Abstract

The familial Alzheimer's disease gene products, presenilin-1 and presenilin-2 (PS1 and PS2), are involved in amyloid beta-protein precursor processing (AbetaPP), Notch receptor signaling, and programmed cell death. However, the molecular mechanisms by which presenilins regulate these processes remain unknown. Clues about the function of a protein can be obtained by seeing whether it interacts with another protein of known function. Using the yeast two-hybrid system, we identified two proteins that interact and colocalize with the presenilins. One of these newly detected presenilin-interacting proteins belongs to the FtsH family of ATP-dependent proteases, and the other one belongs to Rhomboid superfamily of membrane proteins that are highly conserved in eukaryotes, archaea and bacteria. Based on the pattern of amino acid residues conservation in the Rhomboid superfamily, we hypothesize that these proteins possess a metal-dependent enzymatic, possibly protease activity. The two putative proteases interacting with presenilins could mediate specific proteolysis of membrane proteins and contribute to the network of interactions in which presenilins are involved.

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