Structural Biology of Presenilins and Signal Peptide Peptidases

Structural Biology of Presenilins

Published, JBC Papers in Press, April 12, 2013, DOI 10.1074/jbc.R113.463281 Taisuke Tomita and Takeshi Iwatsubo From the Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, and Department of Neuropathology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033 and Core Research for Evolutional Science and Technology, Japan Science and Techno...

Signal peptidases.

Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs.

Recent studies demonstrate that presenilins (PSs) and signal peptide peptidase (SPP) are members of a novel protease family of integral membrane proteins that may utilize a catalytic mechanism similar to classic aspartic proteases such as pepsin, renin and cathepsin D. The defining features of the PSs and SPP are their ability to cleave substrate polypeptides within a transmembrane region, the ...

Signal peptide peptidases and gamma-secretase: cousins of the same protease family?

Signal peptide peptidase (SPP) is an unusual aspartyl protease, which mediates clearance of signal peptides by proteolysis within the endoplasmic reticulum (ER). Like presenilins, which provide the proteolytically active subunit of the gamma-secretase complex, SPP contains a conserved GxGD motif in its C-terminal domain which is critical for its activity. While SPP is known to be an aspartyl pr...

Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD.

In Archaea, the preflagellin peptidase (a type IV prepilin-like peptidase designated FlaK in Methanococcus voltae and Methanococcus maripaludis) is the enzyme that cleaves the N-terminal signal peptide from preflagellins. In methanogens and several other archaeal species, the typical flagellin signal peptide length is 11 to 12 amino acids, while in other archaea preflagellins possess extremely ...