TAILIEUCHUNG - Báo cáo khoa học: Mammalian Gup1, a homolog of Saccharomyces cerevisiae glycerol uptake/transporter 1, acts as a negative regulator for N-terminal palmitoylation of Sonic hedgehog

Mammalian glycerol uptake⁄transporter 1 (Gup1), a homolog of Saccharo-myces cerevisiaeGup1, is predicted to be a member of the membrane-boundO-acyltransferase family and is highly homologous to mammalian hedgehog acyltransferase, known as Skn, the homolog of the Drosoph-ila skinny hedgehog gene product. | ễFEBS Journal Mammalian Gup1 a homolog of Saccharomyces cerevisiae glycerol uptake transporter 1 acts as a negative regulator for N-terminal palmitoylation of Sonic hedgehog Yoichiro Abe1 Yoshiko Kita1 and Takako Niikura1 2 1 Department of Pharmacology Keio University Schoolof Medicine Tokyo Japan 2 Department of Neurology Georgetown University Washington DC USA Keywords Gup1 hedgehog acyltransferase membrane-bound O-acyltransferase palmitoylation Sonic hedgehog Correspondence Y. Abe Department of Pharmacology Keio University Schoolof Medicine 35 Shinanomachi Shinjuku-ku Tokyo 160-8582 Japan Fax 81 3 3359 8889 Tel 81 3 5363 3750 E-mail yoabe@ Present address Department of Neurology Georgetown University Washington DC USA Received 21 August 2007 revised 9 November 2007 accepted 20 November 2007 doi Mammalian glycerol uptake transporter 1 Gup1 a homolog of Saccharo-myces cerevisiae Gup1 is predicted to be a member of the membranebound O-acyltransferase family and is highly homologous to mammalian hedgehog acyltransferase known as Skn the homolog of the Drosophila skinny hedgehog gene product. Although mammalian Gup1 has a sequence conserved among the membrane-bound O-acyltransferase family the histidine residue in the motif that is indispensable to the acyltransferase activity of the family has been replaced with leucine. In this study we cloned Gup1 cDNA from adult mouse lung and examined whether Gup1 is involved in the regulation of N-terminal palmitoylation of Sonic hedgehog Shh . Subcellular localization of mouse Gup1 was indistinguishable from that of mouse Skn detected using the fluorescence of enhanced green fluorescent protein that was fused to each C terminus of these proteins. Gup1 and Skn were co-localized with an endoplasmic reticulum marker 78 kDa glucose-regulated protein suggesting that these two molecules interact with overlapped targets including Shh. In fact full-length Shh coprecipitated with .

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