| Title: | "ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders" |
| Author(s): | Barrowman J; Michaelis S; |
| Address: | "Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA" |
| ISSN/ISBN: | 1437-4315 (Electronic) 1431-6730 (Linking) |
| Abstract: | "ZMPSTE24 is an integral membrane zinc metalloprotease originally discovered in yeast as an enzyme (called Ste24p) required for maturation of the mating pheromone a-factor. Surprisingly, ZMPSTE24 has recently emerged as a key protease involved in human progeroid disorders. ZMPSTE24 has only one identified mammalian substrate, the precursor of the nuclear scaffold protein lamin A. ZMPSTE24 performs a critical endoproteolytic cleavage step that removes the hydrophobic farnesyl-modified tail of prelamin A. Failure to do so has drastic consequences for human health and longevity. Here, we discuss the discovery of the yeast and mammalian ZMPSTE24 orthologs and review the unexpected connection between ZMPSTE24 and premature aging" |
| Keywords: | "Aging, Premature/*genetics Amino Acid Sequence Animals Enzyme Inhibitors/therapeutic use Farnesyltranstransferase/antagonists & inhibitors HIV Protease Inhibitors/pharmacology Humans Lamin Type A/genetics/metabolism Lipoproteins/metabolism Membrane Protei;" |
| Notes: | "MedlineBarrowman, Jemima Michaelis, Susan eng GM41223/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review Germany 2009/05/21 Biol Chem. 2009 Aug; 390(8):761-73. doi: 10.1515/BC.2009.080" |
