MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Other Versions of this Article:
MCB.01226-07v1
28/2/803    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kim, J.-E.
Right arrow Articles by Jang, S. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, J.-E.
Right arrow Articles by Jang, S. K.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, January 2008, p. 803-813, Vol. 28, No. 2
0270-7306/08/$08.00+0     doi:10.1128/MCB.01226-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Proline-Rich Transcript in Brain Protein Induces Stress Granule Formation{triangledown} ,{dagger}

Jung-Eun Kim,1 Incheol Ryu,1 Woo Jae Kim,1 Ok-Kyu Song,2 Jeongeun Ryu,1 Mi Yi Kwon,2 Joon Hyun Kim,1 and Sung Key Jang1*

PBC, Department of Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, Republic of Korea,1 Panbionet Corporation, Pohang, Kyungbuk, Republic of Korea2

Received 10 July 2007/ Returned for modification 17 August 2007/ Accepted 23 October 2007

The repression of translation in environmentally stressed eukaryotic cells causes the sequestration of translation initiation factors and the 40S ribosomal subunit into discrete cytoplasmic foci called stress granules (SGs). Most components of the preinitiation complex, such as eIF3, eIF4A, eIF4E, eIF4G, and poly(A)-binding protein, congregate into SGs under stress conditions. However, the molecular basis of translation factor sequestration into SGs has not been clearly elucidated. Here, we report that proline-rich transcript in brain (PRTB) protein interacts with eIF4G and participates in SG formation. PRTB was recruited to SG under sodium arsenite and heat stress conditions. When overexpressed, PRTB inhibited global translation and formed SGs containing TIA-1, eIF4G, and eIF3. Knockdown of PRTB reduced the SG formation induced by sodium arsenite. These results suggest that PRTB not only is a component of SG formed by cellular stresses but also plays an important role in SG formation via an interaction with the scaffold protein eIF4G, which is associated with many translation factors and mRNAs.


* Corresponding author. Mailing address: PBC, Department of Life Science, Pohang University of Science and Technology, San31, Hyoja-Dong, Pohang 790-784, Republic of Korea. Phone: 82-54-279-2298. Fax: 82-54-279-8009. E-mail: sungkey{at}postech.ac.kr

{triangledown} Published ahead of print on 5 November 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.


Molecular and Cellular Biology, January 2008, p. 803-813, Vol. 28, No. 2
0270-7306/08/$08.00+0     doi:10.1128/MCB.01226-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2008 by the American Society for Microbiology. All rights reserved.