The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2

Paytubi, Sònia; Morrice, Nicholas A.; Boudeau, Jérôme; Proud, Christopher G.

doi:10.1042/bj20070811

Cited by 36 publications

(47 citation statements)

References 18 publications

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“…Our recent data showed that the N terminus of ABC50 was sufficient for its interaction with eIF2 (21). In contrast, the N terminus of ABC50 is not sufficient to mediate association with ribosomes, either NBD1 or NBD2 also being required (21).…”

Section: Discussionmentioning

confidence: 99%

“…Our previous work (2,21) showed that ABC50 interacts with eIF2 and suggested that ABC50 promoted the association of eIF2 with initiator methionyl-tRNA in vitro. This implied that ABC50 probably played a role in mRNA translation, probably at the initiation stage.…”

Section: Discussionmentioning

confidence: 99%

“…HA and GFP antibodies were purchased from Roche Applied Science, actin 20-33 antibody from Sigma, dsRED antibody from Clontech, CAT antibody from 5ЈPrime-3ЈPrime, and antibodies for S6 and rpL28 from Cell Signaling and Santa Cruz Biotechnology, Inc. (Santa Cruz, CA), respectively. Rabbit anti-ABC50 antibodies were obtained as detailed earlier (21). Mouse anti-fibrillarin antibody 72B9 (22) was a kind gift from Prof. E. M. Tan (Scripps Research Institute).…”

Section: Methodsmentioning

confidence: 99%

“…Sheep anti-calregulin antibody was from Santa Cruz Biotechnology. The anti-ABC50 antibody has been described previously (21).…”

Section: Methodsmentioning

confidence: 99%

“…Ribosomes-ABC50 has previously been shown to interact with ribosomes (2), and its NBDs have been shown to be required for this (21). To determine the role of canonical features of the NBDs in this interaction, we created a series of point mutants of ABC50, based on mutations known to interfere with functions of other ABC proteins.…”

Section: Functional Nbds Are Not Required For the Association Of Abc5mentioning

confidence: 99%

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ABC50 Promotes Translation Initiation in Mammalian Cells

Paytubi

Wang

Lam

et al. 2009

Journal of Biological Chemistry

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120

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ABC50 is an ATP-binding cassette (ABC) protein, which, unlike most ABC proteins, does not possess membrane-spanning domains. ABC50 interacts with eukaryotic initiation factor 2 (eIF2), which plays a key role in translation initiation and its control. ABC50 binds to ribosomes, and this interaction requires both the N-terminal domain and at least one ABC domain. Knockdown of ABC50 by RNA interference impaired translation of both cap-dependent and -independent reporters, consistent with a positive role for ABC50 in the function of eIF2, which is required for both types of translation initiation. Mutation of the Walker box A or B motifs in both ABC regions of ABC50 yielded a mutant protein that exerted a dominant-interfering phenotype with respect to protein synthesis and translation initiation. Importantly, although dominant-interfering mutants of ABC50 impaired cap-dependent translation, translation driven by certain internal ribosome entry segments was not inhibited. ABC50 is located in the cytoplasm and nucleoplasm but not in the nucleolus. Thus, ABC50 is not likely to be directly involved in early ribosomal biogenesis, unlike some other ABC proteins. Taken together, the present data show that ABC50 plays a key role in translation initiation and has functions that are distinct from those of other non-membrane ABC proteins.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…Sheep anti-calregulin antibody was from Santa Cruz Biotechnology. The anti-ABC50 antibody has been described previously (21).…”

Section: Methodsmentioning

confidence: 99%

Section: Functional Nbds Are Not Required For the Association Of Abc5mentioning

confidence: 99%

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ABC50 Promotes Translation Initiation in Mammalian Cells

Paytubi

Wang

Lam

et al. 2009

Journal of Biological Chemistry

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120

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ABC‐F translation factors: from antibiotic resistance to immune response

et al. 2020

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Energy-dependent Translational Throttle A (EttA) from E. coli is a paradigmatic ABC-F protein that controls the first step in polypeptide elongation on the ribosome according to the cellular energy status. Biochemical and structural studies have established that ABC-F proteins generally function as translation factors that modulate the conformation of the peptidyl transferase center upon binding to the ribosomal tRNA exit site. These factors, present in both prokaryotes and eukaryotes but not in archaea, use related molecular mechanisms to modulate protein synthesis for heterogenous purposes, ranging from antibiotic resistance and rescue of stalled ribosomes to modulation of the mammalian immune response. Here we review the canonical studies characterizing the phylogeny, regulation, ribosome interactions, and mechanisms of action of the bacterial ABC-F proteins, and discuss the implications of these studies for the molecular function of eukaryotic ABC-F proteins, including the three human family members.

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Proteomic analysis of cellular soluble proteins from human bronchial smooth muscle cells by combining nondenaturing micro 2DE and quantitative LC‐MS/MS. 2. Similarity search between protein maps for the analysis of protein complexes

Jin

Zhang

et al. 2015

Electrophoresis

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Human bronchial smooth muscle cell soluble proteins were analyzed by a combined method of nondenaturing micro 2DE, grid gel‐cutting, and quantitative LC‐MS/MS and a native protein map was prepared for each of the identified 4323 proteins [1]. A method to evaluate the degree of similarity between the protein maps was developed since we expected the proteins comprising a protein complex would be separated together under nondenaturing conditions. The following procedure was employed using Excel macros; (i) maps that have three or more squares with protein quantity data were selected (2328 maps), (ii) within each map, the quantity values of the squares were normalized setting the highest value to be 1.0, (iii) in comparing a map with another map, the smaller normalized quantity in two corresponding squares was taken and summed throughout the map to give an “overlap score,” (iv) each map was compared against all the 2328 maps and the largest overlap score, obtained when a map was compared with itself, was set to be 1.0 thus providing 2328 “overlap factors,” (v) step (iv) was repeated for all maps providing 2328 × 2328 matrix of overlap factors. From the matrix, protein pairs that showed overlap factors above 0.65 from both protein sides were selected (431 protein pairs). Each protein pair was searched in a database (UniProtKB) on complex formation and 301 protein pairs, which comprise 35 protein complexes, were found to be documented. These results demonstrated that native protein maps and their similarity search would enable simultaneous analysis of multiple protein complexes in cells.

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The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2

Cited by 36 publications

References 18 publications

ABC50 Promotes Translation Initiation in Mammalian Cells

ABC50 Promotes Translation Initiation in Mammalian Cells

ABC‐F translation factors: from antibiotic resistance to immune response

Proteomic analysis of cellular soluble proteins from human bronchial smooth muscle cells by combining nondenaturing micro 2DE and quantitative LC‐MS/MS. 2. Similarity search between protein maps for the analysis of protein complexes

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