Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Fujimura-Kamada, K.; Nouvet, F.J.; Michaelis, S.: A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor. J. Cell Biol., 136, 271–285 (1997)
Tam, A.; Nouvet, F.J.; Fujimura-Kamada, K.; Slunt, H.; Sisodia, S.S.; Michaelis, S.: Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing. J. Cell Biol., 142, 635–649 (1998)
Schmidt, W.K.; Tam, A.; Fujimura-Kamada, K.; Michaelis, S.: Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc. Natl. Acad. Sci. USA, 95, 11175–11180 (1998)
Schmidt, W.K.; Tam, A.; Michaelis, S.: Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis. J. Biol. Chem., 275, 6227–6233 (2000)
Tam, A.; Schmidt, W.K,; Michaelis, S.: The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor. J. Biol. Chem., 276, 46798–46806 (2001)
Bracha, K.; Lavy, M.; Yalovsky, S.: The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity. J. Biol. Chem., 277, 29856–29864 (2002)
Boyartchuk, V.L.; Rine, J.: Roles pf prenyl protein proteases in maturation of Saccharomyces cerevisiae. Genetics, 150, 95–1001 (1998)
Leung, G.K.; Schmidt, W.K.; Bergo, M.O.; Gavino, B.; Wong, D.H.; Tam, A.; Ashby, M.N.; Michaelis, S.; Young, S.G.: Biochemical studies of Zmpste24-deficient mice. J. Biol. Chem., 276, 29051–29058 (2001)
Trueblood, C.E.; Boyartchuk, V.L.; Picologlou, E.A.; Rozema, D.; Poulter, C.D.; Rine, J.: The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Mol. Cell. Biol., 20, 4381–4392 (2000)
Boyartchuk, V.L.; Ashby, M.N.; Rine, J.: Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science, 275, 1796–1800 (1997)
Pei, J.; Grishin, N.V.: Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem. Sci., 26, 275–277 (2001)
Corrigan, D.P.; Kuszczak, D.; Rusinol, A.E.; Thewke, D.P.; Hrycyna, C.A.; Michaelis, S.; Sinensky, M.S.: Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24. Biochem. J., 387, 129–138 (2005)
Moulson, C.L.; Go, G.; Gardner, J.M.; van der Wal, A.C.; Smitt, J.H.; van Hagen, J.M.; Miner, J.H.: Homozygous and compound heterozygous mutations in ZMPSTE24 cause the laminopathy restrictive dermopathy. J. Invest. Dermatol., 125, 913–919 (2005)
Varela, I.; Cadinanos, J.; Pendas, A.M.; Gutierrez-Fernandez, A.; Folgueras, A.R.; Sanchez, L.M.; Zhou, Z.; Rodriguez, F.J.; Stewart, C.L.; Vega, J.A.; Tryggvason, K.; Freije, J.M.; Lopez-Otin, C.: Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation. Nature, 437, 564–568 (2005)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2009). Ste24 endopeptidase. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_34
Download citation
DOI: https://doi.org/10.1007/978-3-540-85705-1_34
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-85704-4
Online ISBN: 978-3-540-85705-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)