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Glycobiology Advance Access originally published online on June 16, 2004
Glycobiology 2004 14(10):43R-51R; doi:10.1093/glycob/cwh113
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Glycobiology vol. 14 no. 10 © Oxford University Press 2004; all rights reserved.

REVIEW

Structure and function of vertebrate CMP–sialic acid synthetases

Anja K. Münster-Kühnel2, Joe Tiralongo3, Stephan Krapp4, Birgit Weinhold2, Valentina Ritz-Sedlacek2, Uwe Jacob5 and Rita Gerardy-Schahn1,2

2 Zentrum Biochemie, Abteilung Zelluläre Chemie, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany; 3 Institute for Glycomics, Griffith University, PMB 50 Gold Coast Mail Centre, QLD 9726, Australia; 4 Proteros Biostructures GmbH, Am Klopferspitz 19, D-82152 Martinsried, Germany; and 5 Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany

Received on September 22, 2003; revised on May 18, 2004; accepted on June 10, 2004

Activation of sugars into nucleotide sugars is critical for their entry into biosynthetic pathways. In eukaryotic cells, the activation of the acidic nine-carbon sugar sialic acid to CMP–sialic acid takes place in the cell nucleus, whereas all other nucleotide sugars are made in the cytoplasm. Molecular cloning of vertebrate CMP–sialic acid synthetases confirmed the nuclear localization and introduced new molecular tools for directly exploring the functional mechanisms of the enzymes, as well as the physiological relevance of their nuclear transport. Although major advances have been made in understanding structure–function relationships and defining elements involved in the nuclear transport, the riddle surrounding the physiological relevance of nuclear localization awaits resolution.

1 To whom correspondence should be addressed; e-mail: gerardy-schahn.rita{at}mh-hannover.de


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