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J. Biol. Chem., Vol. 278, Issue 8, 5652-5658, February 21, 2003

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A Diverse Family of Inositol 5-Phosphatases Playing a Role in Growth and Development in Dictyostelium discoideum^*,

Harriët M. Loovers, Kees Veenstra, Helena Snippe, Xavier Pesesse^§, Christophe Erneux^§, and Peter J. M. van Haastert^¶

From the  Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, the Netherlands and ^§ Institute of Interdisciplinary Research, Free University of Brussels, Campus Erasme, Building C, 808 Route de Lennik, B-1070 Brussels, Belgium

Inositol phosphate-containing molecules play an important role in a broad range of cellular processes. Inositol 5-phosphatases participate in the regulation of these signaling molecules. We have identified four inositol 5-phosphatases in Dictyostelium discoideum, Dd5P1-4, showing a high diversity in domain composition. Dd5P1 possesses only a inositol 5-phosphatase catalytic domain. An unique domain composition is present in Dd5P2 containing a RCC1-like domain. RCC1 has a seven-bladed propeller structure and interacts with G-proteins. Dd5P3 and Dd5P4 have a domain composition similar to human Synaptojanin with a SacI domain and OCRL with a RhoGAP domain, respectively. We have expressed the catalytic domains and show that these inositol 5-phosphatases have different substrate preferences. Single and double gene inactivation suggest a functional redundancy for Dd5P1, Dd5P2, and Dd5P3. Inactivation of the gene coding for Dd5P4 leads to defects in growth and development. These defects are restored by the expression of the complete protein but not by the 5-phosphatase catalytic domain.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY184992, AY184993, AY184994, and AY184995.

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