Selkoe, Dennis J

Publication Detail

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A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b.

Regina Fluhrer; Gudula Grammer; Lars Israel; Margaret M Condron; Christof Haffner; Elena Friedmann; Claudia Böhland; Axel Imhof; Bruno Martoglio; David B Teplow; et al. (Profiled Authors: Haass, Christian; Teplow, David B)

Adolf Butenandt Institute, Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig Maximilians University, 80336 Munich, Germany.
Nature cell biology 2006;8(8):894-6.

Gamma-secretase and signal peptide peptidase (SPP) are unusual GxGD aspartyl proteases, which mediate intramembrane proteolysis. In addition to SPP, a family of SPP-like proteins (SPPLs) of unknown function has been identified. We demonstrate that SPPL2b utilizes multiple intramembrane cleavages to liberate the intracellular domain of tumor necrosis factor alpha (TNFalpha) into the cytosol and the carboxy-terminal counterpart into the extracellular space. These findings suggest common principles for regulated intramembrane proteolysis by GxGD aspartyl proteases.

2 Originating Grant

• 1.

  Teplow, David B

  3D Structure of Amyloid beta-Protein Assemblies

  15 February 2002 - 31 January 2008

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 1,920,946

• 2.

  TEPLOW, DAVID B.

  Structural Biology of Amyloid Beta-Protein

  10 December 1998 - 28 February 2015

  NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE

  Total Funding: $ 3,930,754

Scientific Context

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