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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR increased in 2014: 3.268
Rank 106 out of 289 in category Biochemistry & Molecular Biology in the 2014 Thomson Reuters Journal Citation Report/Science Edition

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ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders

Jemima Barrowman1 / Susan Michaelis1

1Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 8, Pages 761–773, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.080, May 2009

Publication History

Received:
2009-02-19
Accepted:
2009-04-15
Published Online:
2009-05-20

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: a-factor; Hutchinson-Gilford Progeria Syndrome (HGPS); mandibuloacral dysplasia (MAD); prelamin A; restrictive dermopathy (RD); Ste24

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[1]
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