Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system.

Wilson, S H; Bailey, A M; Nourse, C R; Mattei, M G; Byrne, J A

Wilson, S H; Bailey, A M; Nourse, C R; Mattei, M G; Byrne, J A.

Afiliación

Wilson SH; Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia.

Genomics ; 76(1-3): 81-8, 2001 Aug.

Article en En | MEDLINE | ID: mdl-11549320

RESUMEN

The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa (35)S-labeled protein which specifically bound full-length GST-Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.

Asunto(s)

Proteínas Portadoras/aislamiento & purificación; Proteínas Portadoras/metabolismo; Proteínas de Transporte de Membrana; Proteínas de la Mielina; Proteínas de Neoplasias/metabolismo; Proteolípidos/aislamiento & purificación; Proteolípidos/metabolismo; Técnicas del Sistema de Dos Híbridos; Proteínas de Transporte Vesicular; Secuencia de Aminoácidos; Neoplasias de la Mama/química; Proteínas Portadoras/genética; Mapeo Cromosómico/métodos; Cromosomas Humanos Par 8/genética; ADN Complementario/genética; Glutatión Transferasa/genética; Glutatión Transferasa/metabolismo; Humanos; Datos de Secuencia Molecular; Proteínas Proteolipídicas Asociadas a Mielina y Linfocito; Proteínas de Neoplasias/genética; Unión Proteica/genética; Transporte de Proteínas/genética; Proteolípidos/química; Proteolípidos/genética; ARN Mensajero/genética; ARN Mensajero/metabolismo; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Células Tumorales Cultivadas

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Proteolípidos / Proteínas Portadoras / Técnicas del Sistema de Dos Híbridos / Proteínas de Transporte Vesicular / Proteínas de la Mielina / Proteínas de Neoplasias Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Genomics Asunto de la revista: GENETICA Año: 2001 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Estados Unidos

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