Biophysics

Intramembrane-Cleaving Proteases (I-CLiPs) (Proteases in by Nigel M. Hooper (Editor), Uwe Lendeckel (Editor)

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By Nigel M. Hooper (Editor), Uwe Lendeckel (Editor)

In recent times increasingly more proteases were pointed out that catalyse peptide bond hydrolysis within the aircraft of the mobile membrane. those so-called intramembrane-cleaving proteases (I-CLiPs) are all in favour of a various diversity of mobile techniques, together with mobile legislation, signalling, quorum sensing, protein processing, lipid metabolism and the spread out protein reaction. a few I-CLiPs play serious roles in illnesses resembling Alzheimer s and viral an infection. The authors, who're all global leaders during this intriguing box of telephone biology, offer an outline of a few of the proteases together with contemporary info derived from the structural choice of a few of the I-CliPs, and talk about a number of the roles that those proteases play in biology and affliction. the purpose of this publication is to supply an replace in this rising crew of surprising yet very important proteases for either the professional and people with a broader curiosity in proteases. among the objective viewers might be protease researchers, enzymologists, these operating in academia and the pharmaceutical on organic methods and illnesses related to I-CLiPs.

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Nyborg A. , Ladd T. , Kukar T. and Golde T. E. (2006a) Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase. FASEB J 20, 1671–1679. Nyborg A. , Ladd T. , Zwizinski C. , Lah J. J. and Golde T. E. (2006b) Sortilin, SorCS1b, and SorLA Vps10p sorting receptors, are novel gamma-secretase substrates. Mol Neurodegener 1, 3. Nyborg A. , Kornilova A. , Ladd T. , Wolfe M. S. and Golde T. E. (2004b) Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor.

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2005). The prevailing picture is that cleavage may start from the cytosolic border of the membrane at the -site and then proceed in a stepwise manner via the -site to the -site by cleavage after every third amino acid on one side of the -helical TMD (Qi-Takahara et al. 2005). However, although probably less likely, the other two possible directions of the cleavage, from to to , or alternatively starting from the -site and then proceeding from this site in two opposite directions to and cannot be fully excluded as, for example, APP mutants that block cleavage at either of the two major sites, and , have not been identified.

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