The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.
The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.
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DOI:
10.1111/j.1600-0854.2010.01089.x
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发表时间:
2010-09
期刊:
影响因子:
--
通讯作者:
Glick BS
中科院分区:
文献类型:
--
作者:
Levi SK;Bhattacharyya D;Strack RL;Austin JR 2nd;Glick BS
In mammalian cells, the “Golgi Reassembly and Stacking Protein” (GRASP) family has been implicated in Golgi stacking, but the broader functions of GRASP proteins are still unclear. The yeast Saccharomyces cerevisiae contains a single nonessential GRASP homolog called Grh1. However, Golgi cisternae in S. cerevisiae are not organized into stacks, so a possible structural role for Grh1 has been difficult to test. Here we examined the localization and function of Grh1 in S. cerevisiae and in the related yeast Pichia pastoris, which has stacked Golgi cisternae. In agreement with earlier studies indicating that Grh1 interacts with COPII vesicle coat proteins, we find that Grh1 colocalizes with COPII at transitional ER (tER) sites in both yeasts. Deletion of P. pastoris Grh1 had no obvious effect on the structure of tER-Golgi units. To test the role of S. cerevisiae Grh1, we exploited the observation that inhibiting ER export in S. cerevisiae generates enlarged tER sites that are often associated with the cis-Golgi. This tER-Golgi association was preserved in the absence of Grh1. The combined data suggest that Grh1 acts early in the secretory pathway but is dispensable for the organization of secretory compartments.
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DOI:
10.1083/jcb.200607151
发表时间:
2007-01-29
期刊:
The Journal of cell biology
影响因子:
--
作者:
Behnia R;Barr FA;Flanagan JJ;Barlowe C;Munro S
通讯作者:
Munro S
影响因子:
4.8
作者:
Bachert, Collin;Linstedt, Adam D.
通讯作者:
Linstedt, Adam D.
影响因子:
9.2
作者:
Connerly, PL;Esaki, M;Glick, BS
通讯作者:
Glick, BS
影响因子:
7.8
作者:
FRANZUSOFF, A;REDDING, K;SCHEKMAN, R
通讯作者:
SCHEKMAN, R
影响因子:
64.5
作者:
KUNZ, J;HENRIQUEZ, R;HALL, MN
通讯作者:
HALL, MN