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J. Biol. Chem., Vol. 281, Issue 28, 19339-19345, July 14, 2006

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Physical and Functional Association of Human Protein O-Mannosyltransferases 1 and 2^*

Keiko Akasaka-Manya, Hiroshi Manya, Ai Nakajima, Masao Kawakita, and Tamao Endo¹

From the Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, Tokyo 173-0015, Japan and Department of Applied Chemistry, Kogakuin University, Tokyo 163-8677, Japan

A defect of protein O-mannosylation causes congenital muscular dystrophy with brain malformation and structural eye abnormalities, so-called Walker-Warburg syndrome. Protein O-mannosylation is catalyzed by protein O-mannosyltransferase 1 (POMT1) and its homologue, POMT2. Coexpression of POMT1 and POMT2 is required to show O-mannosylation activity. Here we have shown that POMT1 forms a complex with POMT2 and the complex possesses protein O-mannosyltransferase activity. Results indicate that POMT1 and POMT2 associate physically and functionally in vivo. Recently, three mutations were reported in the POMT1 gene of patients who showed milder phenotypes than typical Walker-Warburg syndrome. We coexpressed these mutant POMT1s with POMT2 and found that none of them had any activity. However, all POMT1 mutants, including previously identified POMT1 mutants, coprecipitated with POMT2. These results indicate that the mutant POMT1s could form heterocomplexes with POMT2 but that such complexes are insufficient for enzymatic activity.

Received for publication, February 6, 2006 , and in revised form, May 12, 2006.

^* This work was supported by Research Grant 17A-10 for Nervous and Mental Disorders and Research on Psychiatric and Neurological Diseases and Mental Health from the Ministry of Health, Labor and Welfare of Japan, Grant-in-aid 14082209 for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science, and Technology of Japan, and the Japan Society for the Promotion of Science Core-to-Core Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Glycobiology Research Group, Tokyo Metropolitan Inst. of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, 35-2 Sakaecho, Itabashi-ku, Tokyo 173-0015, Japan. Tel.: 81-3-3964-3241 (ext. 3080); Fax: 81-3-3579-4776; E-mail: endo{at}tmig.or.jp.

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