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J. Biol. Chem., Vol. 279, Issue 41, 42535-42544, October 8, 2004

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Heat Shock Induces Preferential Translation of ERGIC-53 and Affects Its Recycling Pathway^*

Carmen Spatuzza, Maurizio Renna, Raffaella Faraonio, Giorgia Cardinali¶, Gianluca Martire||, Stefano Bonatti**, and Paolo Remondelli**

From the Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, I-80131, Naples, Italy, the ^¶Istituto Dermatologico San Gallicano, I-00144, Rome, Italy, the ^||Dipartimento di Scienze e Tecnologie dell'Ambiente e del Territorio, Università del Molise, I-86170, Isernia, Italy, and the Dipartimento di Scienze Farmaceutiche, Università degli Studi di Salerno, I-84034, Fisciano-Salerno, Italy

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.

Received for publication, February 19, 2004 , and in revised form, July 15, 2004.

^* This work was supported in part by grants from MIUR (PRIN 2002 and 03) and from CIB (2003) (to S. B.), and from the Università di Salerno (ex 60% 2003 and 2004) (to P. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplementary Materials.

^** These authors contributed equally to the work.

To whom correspondence should be addressed. Tel.: 39-089-962627; Fax: 39-089-962828; E-mail: premondelli{at}unisa.it.

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