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Glycobiology Advance Access published online on June 16, 2004
Glycobiology, doi:10.1093/glycob/cwh113
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Received September 22, 2003
Revised May 18, 2004
Accepted June 10, 2004

REVIEW

Structure and function of vertebrate CMP-sialic acid synthetases

Anja K. Münster-Kühnel 1, Joe Tiralongo 2, Stephan Krapp 3, Birgit Weinhold 1, Valentina Ritz-Sedlacek 1, Uwe Jacob 4, Rita Gerardy-Schahn 1*

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

* To whom correspondence should be addressed. E-mail: gerardy-schahn.rita{at}mh-hannover.de.


  Abstract

Activation of sugars into nucleotide sugars is pivotal 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, while all other nucleotide sugars are made in the cytoplasm. Molecular cloning of vertebrate CMP-sialic acid synthetases confirmed the nuclear localisation and introduced new molecular tools for directly exploring the functional mechanisms of the enzymes, as well as the physiological relevance of their nuclear transport. While major advance has been made in understanding structure-function-relationships and in defining elements involved in the nuclear transport, the riddle surrounding the physiological relevance of nuclear localisation awaits resolution.


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