生物
高尔基体
分泌物
复印机
G蛋白
细胞生物学
分泌途径
生物化学
信号转导
细胞
作者
Antti Salminen,Peter Novick
出处
期刊:Cell
[Elsevier]
日期:1987-05-01
卷期号:49 (4): 527-538
被引量:871
标识
DOI:10.1016/0092-8674(87)90455-7
摘要
Secretion is blocked at the post-Golgi stage within 5 min of a shift of sec4-8 cells from 25 degrees C to 37 degrees C. Analysis of SEC4 predicts a protein product of 23.5 kd molecular weight that shares 32% homology with ras proteins and is essential for growth. The regions of best homology are those involved in the binding and hydrolysis of GTP. Duplication of SEC4 suppresses post-Golgi-blocked mutations in three sec genes. These mutations are lethal when combined with sec4-8 at 25 degrees C. Mutations that block elsewhere on the pathway are not suppressed by the SEC4 duplication and are not lethal when combined with sec4-8. We propose that the SEC4 product is a GTP-binding protein that plays an essential role in controlling a late stage of the secretory pathway.
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