A resident Golgi protein is excluded from peri-Golgi vesicles in NRK cells

被引:51
作者
Cosson, P
Amherdt, M
Rothman, JE
Orci, L [1 ]
机构
[1] Univ Geneva, Sch Med, Dept Morphol, CH-1211 Geneva 4, Switzerland
[2] Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA
关键词
Golgi apparatus; cisternal maturation; coatomer; glycosyltransferase; secretion;
D O I
10.1073/pnas.192460999
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
To understand the structure and the function of the Golgi apparatus, it is essential to establish how resident Golgi enzymes are localized in only a few Golgi cisternae. In particular it is crucial to establish whether Golgi enzymes are retained specifically in cisternae, or if they are continuously transported from cisterna to cisterna. Here we report that a resident Golgi enzyme is largely excluded from peri-Golgi transport vesicles in normal rat kidney cells, a cell type in which conflicting results have been reported. Analysis of the lateral distribution of two markers within Golgi cisternae led to the same conclusion: a protein incorporated in vesicles (KDEL receptor) is concentrated at the rims of cisternae where vesicles form, while mannosidase II is not. These results suggest that localization of resident Golgi enzymes is achieved primarily by selective retention within cisternae and exclusion from transport vesicles. These observations cannot easily be reconciled with the vision of rapidly maturing Golgi cisternae as the principal means of intra-Golgi transport.
引用
收藏
页码:12831 / 12834
页数:4
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