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Journal of Cell Science 114, 3991-4000 (2001)
© 2001 The Company of Biologists Limited

RESEARCH ARTICLE

FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments

S. H. Ridley1, N. Ktistakis1, K. Davidson1, K. E. Anderson1, M. Manifava1, C. D. Ellson1, P. Lipp2, M. Bootman2, J. Coadwell1, A. Nazarian3, H. Erdjument-Bromage3, P. Tempst3, M. A. Cooper4, J. W. J. F. Thuring4, Z.-Y. Lim4, A. B. Holmes4, L. R. Stephens1 and P. T. Hawkins1,*

1 Inositide Laboratory, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK
2 Laboratory of Molecular Signalling, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK
3 Memorial Sloan-Kettering Cancer Center, New York, NY10021, USA
4 Department of Chemistry, Cambridge University, Lensfield Road, Cambridge CB2 1EW, UK

*Author for correspondence (e-mail: phillip.hawkins{at}bbsrc.ac.uk)

Accepted July 26, 2001

FENS-1 and DFCP1 are recently discovered proteins containing one or two FYVE-domains respectively. We show that the FYVE domains in these proteins can bind PtdIns3P in vitro with high specificity over other phosphoinositides. Exogenously expressed FENS-1 localises to early endosomes: this localisation requires an intact FYVE domain and is sensitive to wortmannin inhibition. The isolated FYVE domain of FENS-1 also localises to endosomes. These results are consistent with current models of FYVE-domain function in this cellular compartment. By contrast, exogenously expressed DFCP1 displays a predominantly Golgi, endoplasmic reticulum (ER) and vesicular distribution with little or no overlap with FENS-1 or other endosomal markers. Overexpression of DFCP1 was found to cause dispersal of the Golgi compartment defined by giantin and gpp130-staining. Disruption of the FYVE domains of DFCP1 causes a shift to more condensed and compact Golgi structures and overexpression of this mutant was found to confer significant protection to the Golgi against brefeldin-induced dispersal. These properties of DFCP1 are surprising, and suggest FYVE domain-localisation and function may not be exclusively endosomal.

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Key words: FYVE domain, PtdIns3P, Endosomes, Golgi, Vesicle trafficking


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© The Company of Biologists Ltd 2001