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Papers In Press, published online ahead of print January 16, 2002
Chemistry (M/C 111), Univ. of Illinois at Chicago, Chicago, IL 60607-7061
Corresponding Author: wcho{at}uic.edu
The activation of 5-lipoxygenase (5-LO) involves its calcium-dependent translocation to the nuclear envelope at which it catalyzes the two-step transformation of arachidonic acid into leukotriene A4, which then leads to the synthesis of various leukotrienes. To understand the mechanism by which the 5-LO is specifically targeted to the nuclear envelope, we studied the membrane binding properties of the amino-terminal domain of 5-LO that has been proposed to have a C2 domain-like structure. The model building, the electrostatic potential calculation, and the in vitro membrane binding studies of the isolated C2-like domain of 5-LO and selected mutants show that this Ca2+-dependent domain selectively binds zwitterionic phosphatidylcholine, which is conferred by tryptophan residues (Trp13, Trp75, and Trp102) located in the putative Ca2+-binding loops. The spatiotemporal dynamics of the enhanced green fluorescence protein-tagged C2-like domain of 5-LO domain and mutants in living cells also shows that its phosphatidylcholine selectivity accounts for the specific targeting of 5-LO to the nuclear envelope. Together, these results show that the C2-like domain of 5-LO is a genuine Ca2+-dependent membrane targeting domain and that the subcellular localization of the domain is governed in large part by its membrane binding properties.
J. Biol. Chem, 10.1074/jbc.M112393200
Submitted on December 26, 2001
Revised on January 16, 2002
Accepted on January 16, 2002
A molecular basis of specific subcellular localization of the C2-like domain of 5-lipoxygenase
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