The eukaryotic translation initiation factor 3f (eIF3f) interacts physically with the alpha 1B-adrenergic receptor and stimulates adrenoceptor activity.

Q2 Biochemistry, Genetics and Molecular Biology BMC Biochemistry Pub Date : 2015-10-23 DOI:10.1186/s12858-015-0054-5
Mario Javier Gutiérrez-Fernández, Ana Edith Higareda-Mendoza, César Adrián Gómez-Correa, Marco Aurelio Pardo-Galván
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引用次数: 5

Abstract

Background: eIF3f is a multifunctional protein capable of interacting with proteins involved in different cellular processes, such as protein synthesis, DNA repair, and viral mRNA edition. In human cells, eIF3f is related to cell cycle and proliferation, and its deregulation compromises cell viability.

Results: We here report that, in native conditions, eIF3f physically interacts with the alpha 1B-adrenergic receptor, a plasma membrane protein considered as a proto-oncogene, and involved in vasoconstriction and cell proliferation. The complex formed by eIF3f and alpha 1B-ADR was found in human and mouse cell lines. Upon catecholamine stimulation, eIF3f promotes adrenoceptor activity in vitro, independently of the eIF3f proline- and alanine-rich N-terminal region.

Conclusions: The eIF3f/alpha adrenergic receptor interaction opens new insights regarding adrenoceptor-related transduction pathways and proliferation control in human cells. The eIf3f/alpha 1B-ADR complex is found in mammals and is not tissue specific.

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真核生物翻译起始因子3f (eIF3f)与α 1b肾上腺素能受体相互作用,刺激肾上腺素能受体活性。
背景:eIF3f是一种多功能蛋白,能够与参与不同细胞过程的蛋白相互作用,如蛋白质合成、DNA修复和病毒mRNA编辑。在人类细胞中,eIF3f与细胞周期和增殖有关,其失调会损害细胞活力。结果:我们在这里报道,在自然条件下,eIF3f与α 1b肾上腺素能受体相互作用,α 1b肾上腺素能受体是一种被认为是原癌基因的质膜蛋白,参与血管收缩和细胞增殖。在人和小鼠细胞系中均发现了eIF3f与α 1B-ADR形成的复合物。在儿茶酚胺刺激下,eIF3f在体外促进肾上腺素受体活性,独立于eIF3f富含脯氨酸和丙氨酸的n端区域。结论:eIF3f/ α肾上腺素能受体的相互作用为肾上腺素受体相关的转导途径和人类细胞的增殖控制提供了新的见解。eIf3f/ α 1B-ADR复合体存在于哺乳动物中,不具有组织特异性。
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来源期刊
BMC Biochemistry
BMC Biochemistry BIOCHEMISTRY & MOLECULAR BIOLOGY-
CiteScore
4.80
自引率
0.00%
发文量
0
审稿时长
3 months
期刊介绍: BMC Biochemistry is an open access journal publishing original peer-reviewed research articles in all aspects of biochemical processes, including the structure, function and dynamics of metabolic pathways, supramolecular complexes, enzymes, proteins, nucleic acids and small molecular components of organelles, cells and tissues. BMC Biochemistry (ISSN 1471-2091) is indexed/tracked/covered by PubMed, MEDLINE, BIOSIS, CAS, EMBASE, Scopus, Zoological Record, Thomson Reuters (ISI) and Google Scholar.
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