Heat shock induces preferential translation of ERGIC-53 and affects its recycling pathway

被引:22
作者
Spatuzza, C
Renna, M
Faraonio, R
Cardinali, G
Martire, G
Bonatti, S
Remondelli, P [1 ]
机构
[1] Univ Naples Federico II, Dipartimento Biochim & Biotecnol Med, I-80131 Naples, Italy
[2] Ist Dermatol S Maria & S Gallicano, I-00144 Rome, Italy
[3] Univ Molise, Dipartimento Sci & Tecnol Ambiente & Terr, I-86170 Isernia, Italy
[4] Univ Salerno, Dipartimento Sci Farmaceut, I-84034 Fisciano Salerno, Italy
关键词
D O I
10.1074/jbc.M401860200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
ERGIC-53 is a lectin-like transport receptor protein, which recirculates between the ER and the Golgi complex and is required for the intracellular transport of a restricted number of glycoproteins. We show in this article that ERGIC-53 accumulates during the heat shock response. However, at variance with the unfolded protein response, which results in enhanced transcription of ERGIC-53 mRNA, heat shock leads only to enhanced translation of ERGIC-53 mRNA. In addition, the half-life of the protein does not change during heat shock. Therefore, distinct signal pathways of the cell stress response modulate the ERGIC-53 protein level. Heat shock also affects the recycling pathway of ERGIC-53. The protein rapidly redistributes in a more peripheral area of the cell, in a vesicular compartment that has a lighter sedimentation density on sucrose gradient in comparison to the compartment that contains the majority of ERGIC-53 at 37 C. This effect is specific, as no apparent reorganization of the endoplasmic reticulum, intermediate compartment and Golgi complex is morphologically detectable in the cells exposed to heat shock. Moreover, the anterograde transport of two unrelated reporter proteins is not affected. Interestingly, MCFD2, which interacts with ERGIC-53 to form a complex required for the ER-to-Golgi transport of specific proteins, is regulated similarly to ERGIC-53 in response to cell stress. These results support the view that ERGIC-53 alone, or in association with MCFD2, plays important functions during cellular response to stress conditions.
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收藏
页码:42535 / 42544
页数:10
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