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Las mutaciones en la vía de la CDP-colina para la biosíntesis de fosfolípidos eluden el requisito de una proteína

A E Cleves¹, T P McGee, E A Whitters

¹Department of Microbiology, University of Illinois, Urbana-Champaign 61801.

|February 22, 1991

Resumen

La proteína SEC14p es esencial para la función secretora de la levadura Golgi. La disrupción de la colina quinasa (CKI) eludió este requisito SEC14p, revelando un vínculo entre la biosíntesis de fosfolípidos y la función de Golgi.

Área de la Ciencia:

Biología celular Biología celular.
Biología Molecular Biología Molecular
La bioquímica es la bioquímica.

Sus antecedentes:

SEC14p es una proteína de transferencia de fosfatidilinositol (PI) / fosfatidilcolina (PC) de levadura.
SEC14p es crucial para estimular la función secretora de Golgi de la levadura.

Objetivo del estudio:

Para investigar la localización de SEC14p.
Para identificar los genes que pueden eludir el requisito esencial para SEC14p.
Para comprender la influencia de la biosíntesis de fosfolípidos en la función de Golgi de la levadura.

Principales métodos:

Estudios de localización de SEC14p en la levadura Golgi.
Cribado genético para mutaciones supresoras que eluden el requisito SEC14p.
Análisis de los efectos de alteración genética de la colina quinasa (CKI).

Principales resultados:

Se encontró que SEC14p se localiza en la levadura Golgi.
Las mutaciones en seis genes eludieron el requisito SEC14p.
La alteración del gen de la colina quinasa (CKI) hizo que las células fueran independientes de SEC14p.
El producto del gen CKI antagoniza la función SEC14p.

Conclusiones:

SEC14p controla el contenido de fosfolípidos en las membranas de Golgi de la levadura.
La biosíntesis a través de la vía CDP-colina influye en la función de Golgi de la levadura.
Existe un nuevo vínculo entre la biosíntesis de fosfolípidos y la regulación de Golgi mediada por SEC14p.

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