Galactosyltransferase--still up and running.
The following review on galactosyltransferase (gal-T1) intends to cover genetic, biochemical, structural, biotechnological, cell biological and medical aspects of this enzyme in a comprehensive manner from discovery to the present day which have brought to light a genetic defect of this enzyme. Early work has only been included if it appeared relevant to ongoing issues. Following the evolution of a research topic over 40 years is in itself a fascinating endeavor as it permits to observe the ins and outs of hypotheses, fashions and errors. Gal-T1 is a beautiful example as it has been involved in almost every aspect of life science. Importantly, there is a future to this enzyme as a research topic, since many questions still remain unanswered: to which extent is it a representative Golgi protein? What is the role of the gene family of gal-Ts? Does gal-T1 exert any functions other than a catalytic one? Why is it phosphorylated? Does it form homodimers in vivo? Surely, there is room for further work, which is likely to reveal further insights into cellular trafficking and signaling and, in the context of the gene family, shall contribute to understanding development and morphogenesis.
Berger
E G
EG
Institute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland. egberger@physiol.unizh.ch
Rohrer
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology; D005700:Galactosyltransferases / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007120:Immunochemistry; D051379:Mice; D018345:Mice, Knockout; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D011994:Recombinant Proteins; D005700:Galactosyltransferases