ABCE1 Membrane Protein Introduction

Introduction of ABCE1

ABCE1, also known as ABC38, OABP, RNASEL1, RNASELI, ribonuclease L (2,5-Oligoisoadenylate synthetase-dependent) inhibitor, or ATP-binding cassette, sub-family E (OABP), member 1, is a 67.3 kDa transport protein that is composed by 599 amino acids. In humans, it is encoded by the ABCE3 gene located at the chromosome 4q31.21. ABCE1 as an ATPase belongs to a superfamily of ATP-binding cassette (ABC) transporters and an OABP subfamily. So far, there are 49 human transporters of ABC families have been identified, performing various functions in cells and mediating the transport of specific substrates across biological membranes, including sugar, lipids, and chloride. The protein sequences of ABCE1 between species are very well conserved, for instance, Pixie and yeast Rli1p shares 66% identity, and Rli1p and human ABCR1 have 67% identity.

Function of ABCE1 Membrane Protein

ABCE1 has a cysteine-rich N-terminal region that is supposed to tightly bind two [4Fe-4S] clusters. Depletion of available Fe/S clusters or mutation of this region renders the protein unable to function and loss of cell viability, which confers ABCE1 the only known important cytoplasmic protein dependent on the Fe/S cluster biosynthesis in mitochondria. The ABCE1 protein was initially described as a ribonuclease L inhibitor (RNase L Inhibitor). Recent evidence has identified ABCE1 as a ribosome-recycling factor essential for the translation initiation, elongation, termination, as well as ribosome recycling in eukaryotes. As a negative regulator of the 2-5A (5'-phosphorylated 2', 5'-linked oligoadenylates)/RNase L system, ABCE1 is able to regulate the RNA stability of cell and may be implicated in a wide range of biological functions, such as viral infection and tumor cell proliferation. Later, this protein is manifested as a host factor critical for the assembly of primate lentivirus capsids, especially for human immunodeficiency virus-1 (HIV-1).

Fig.1 Interactions of ABCE1 with the small 40S ribosomal subunit. (Heuer, 2017)

Application of ABCE1 Membrane Protein in Literature

1. Wu Z., et al. Ubiquitination of ABCE1 by NOT4 in response to mitochondrial damage links co-translational quality control to PINK1-directed mitophagy. Cell Metab. 2018, 8(1), 130-144.e7. PubMed ID: 29861391
   
   

   This study showed that ribosome-correlated co-translational quality control forms an early signal to trigger mitophagy. The final results have demonstrated extensive therapeutic implications for further understanding and treatments of neurodegenerative diseases.

2. Mancera-Martínez E., et al. ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation. RNA Biol. 2017, 14(10), 1279-1285. PubMed ID: 28498001
   
   

   Based on an analysis of published late-stage 48S initiation complex from rabbit, this paper provided new mechanistic views about this putative role of ABCE1 in initiation. This point of opinion represented the first structural evidence in which the regulatory function of this recycling factor ABCE1 in initiation is discussed.

3. Heuer A., et al. Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. Nat Struct Mol Biol. 2017, 24(5), 453-460. PubMed ID: 28368393
   
   

   ABCE1, an important ATP-binding cassette (ABC) protein, splits 80S ribosomes into 60S and 40S subunits after classical termination or quality-control-based mRNA surveillance events. Nevertheless, the underlying splitting mechanism is still enigmatic. Thus, this review presented a cryo-EM structure of yeast 40S-ABCE1 post-splitting complex at 3.9-Å resolution.

4. Wei D., et al. Genistein suppresses retinoblastoma cell viability and growth and induces apoptosis by upregulating miR-145 and inhibiting its target ABCE1. Mol Vis. 2017, 23, 385-394. PubMed ID: 28706438
   
   

   Retinoblastoma is known as a rare malignancy in developing retina tissue of children with limited therapeutic choices. This paper tried to investigate underlying clinical values of genistein, that is a phytoestrogen derived from soybeans with antioxidant activity.

5. Yu Q., et al. Deficiency of functional iron-sulfur domains in ABCE1 inhibits the proliferation and migration of lung adenocarcinomas by regulating the biogenesis of beta-actin in vitro. Cell Physiol Biochem. 2017, 44(2), 554-566. PubMed ID: 29145194
   
   

   The results in this study demonstrated an indispensable role of Fe-S clusters when ABCE1 involves in the proliferation and the migration of LUADs through interacting with β-actin. The Fe-S cluster of ABCE1 may be a potential target for the prevention of lung adenocarcinoma metastasis.

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Reference

1. Heuer A, et al. (2017). Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. Nat Struct Mol Biol. 24(5), 453-460.

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