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J Biol Chem, Vol. 273, Issue 31, 19602-19611, July 31, 1998

A Formiminotransferase Cyclodeaminase Isoform Is Localized to the Golgi Complex and Can Mediate Interaction of Trans-Golgi Network-derived Vesicles with Microtubules

Dagmar HennigDagger , Suzie J. Scales, Anne MoreauDagger , Laura L. Murleyparallel , Jan De MeyDagger , and Thomas E. Kreis

From the Dagger  Department of Supramolecular and Cell Biology, Institut Jacques Monod, 2 Place Jussieu, 75251 Paris, France,  Department of Cell Biology, University of Geneva, Sciences III, 30 Quai Ernest-Ansermet, 1211 Geneva 4, Switzerland, and parallel  Department of Biochemistry, McGill University, Montréal, Québec H3G 1Y6, Canada

A protein of 60 kDa (p60) has been identified using a quantitative in vitro vesicle-microtubule binding assay. Purified p60 induces co-sedimentation with microtubules of trans-Golgi network-derived vesicles isolated from polarized, perforated Madin-Darby canine kidney cells. Sequencing of the cDNA coding for this protein revealed that it is the chicken homologue of formiminotransferase cyclodeaminase (FTCD), a liver-specific enzyme involved in the histidine degradation pathway. Purified p60 from chicken liver has formiminotransferase activity, confirming that it is FTCD or an isoform of this enzyme. Isoforms of FTCD were identified in chicken hepatoma and HeLa cells, and immunolocalize to the region of the Golgi complex and vesicular structures in its vicinity. Furthermore, 58K, a previously identified microtubule-binding Golgi protein from rat liver (Bloom, G. S., and Brashear, T. A. (1989) J. Biol. Chem. 264, 16083-16092), is identical to FTCD. Both proteins co-purify with microtubules and co-localize with membranes of the Golgi complex. The capacity of FTCD to bind both to microtubules and Golgi-derived membranes may suggest that this protein, or one of its isoforms, might have in addition to its enzymatic activity, a second physiological function in mediating interaction of Golgi-derived membranes with microtubules.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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