Letter to the Editor: NMR structure of human coactosin-like protein

Abstract

Key words: coactosin-like protein, human CLP, NMR structureBiological contextThe human Coactosin-Like Protein (CLP) genewas initially found as a sequence flanking a deletionon the human chromosome 17 characterizing theSmith-Magenis syndrome (Chen et al., 1997). Theencoded CLP protein (142 amino acids, 16 kDa) issimilar to D. Discoideum coactosin (de Hostoset al., 1993) which is a member of the ADF/Cofilingroup of actin binding proteins (Lappalainen et al.,1998). Coactosin can bind to filamentous actin (F-actin) (de Hostos et al., 1993) and interfere withcapping of actin filaments (Rohrig et al., 1995),thereby promoting actin polymerization.Similarly, human CLP was characterized asan F-actin binding protein that colocalized withactin stress fibers in transfected mammalian(CHO and Cos-7) cells. Site-directed mutagenesisstudies revealed the essential role of Lys75, a res-idue highly conserved in related proteins, inmediating F-actin binding (Provost et al., 2001b).Most interestingly, human CLP also binds to5-lipoxygenase (5LO; Provost et al., 1999, 2001b)which plays an important role in leukotrienebiosynthesis, converting arachidonic acid to5(S)-hydroperoxy-6,8,11,14-eicosatetraenoic acid(5-HPETE) and subsequently to the epoxide leu-kotriene (LT) A