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https://hdl.handle.net/2440/82723
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Type: | Journal article |
Title: | The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2 |
Author: | Paytubi, S. Morrice, N. Boudeau, J. Proud, C. |
Citation: | Biochemical Journal, 2008; 409(1):223-231 |
Publisher: | Portland Press |
Issue Date: | 2008 |
ISSN: | 0264-6021 1470-8728 |
Statement of Responsibility: | Sonia Paytubi, Nicholas A. Morrice, Jerome Boudeau and Christopher G. Proud |
Abstract: | ABC50 is an ABC (ATP-binding cassette) protein which, unlike most ABC proteins, lacks membrane-spanning domains. ABC50 interacts with eIF2 (eukaryotic initiation factor 2), a protein that plays a key role in translation initiation and in its control, and in regulation of ribosomes. Here, we establish that the interaction of ABC50 with eIF2 involves features in the N-terminal domain of ABC50, the region of ABC50 that differs most markedly from other ABC proteins. This region also shows no apparent similarity to the eIF2-binding domains of other partners of eIF2. In contrast, the N-terminus of ABC50 cannot bind to ribosomes by itself, but it can in conjunction with one of the nucleotide-binding domains. We demonstrate that ABC50 is a phosphoprotein and is phosphorylated at two sites by CK2. These sites, Ser-109 and Ser-140, lie in the N-terminal part of ABC50 but are not required for the binding of ABC50 to eIF2. Expression of a mutant of ABC50 in which both sites are mutated to alanine markedly decreased the association of eIF2 with 80S ribosomal and polysomal fractions. |
Keywords: | ABC protein, CK2, eIF2, ribosome, translation initiation |
Rights: | © The Authors |
DOI: | 10.1042/BJ20070811 |
Published version: | http://dx.doi.org/10.1042/bj20070811 |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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