PABPC1

Official Full Name

poly(A) binding protein cytoplasmic 1

Organism

Homo sapiens

GeneID

26986

Background

This gene encodes a poly(A) binding protein. The protein shuttles between the nucleus and cytoplasm and binds to the 3' poly(A) tail of eukaryotic messenger RNAs via RNA-recognition motifs. The binding of this protein to poly(A) promotes ribosome recruitment and translation initiation; it is also required for poly(A) shortening which is the first step in mRNA decay. The gene is part of a small gene family including three protein-coding genes and several pseudogenes.[provided by RefSeq, Aug 2010]

Synonyms

PAB1; PABP; PABP1; PABPC2; PABPL1;

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Detailed Information

Prognostic value of PABPC1 in gliomas manifested by its bioinformatic profiling

In the updated 2016 WHO classification system of CNS, the most prevalent and fatal brain tumor in adults, gliomas have been categorized by histology and molecular parameters into as followed: isocitrate dehydrogenase (IDH) mutated lower grade gliomas (LGG) with or without 1p/19q-codel, IDH-wildtype LGG, IDH mutated or not glioblastoma multiforme (GBM). The work of identifying novel biomarkers or targets seems to be crucial for the purpose of diagnostic accuracy and treatment efficacy improvement.

Due to the specifically bounding with the poly adenosine tail of RNA, PABPs play essential roles in the initiation of translation a stabilization of mRNA. Among those PABPs included functional proteins in human, PABP1 is encoded by the PABPC1 gene. There is over-expression of PABPC1 in esophageal cancer, gastric carcinoma, follicular thyroid cancer, bladder cancer and so on, while with little genetic and epigenetic features coverage of PABPC1 in gliomas. The exploration of clinical and molecular characteristics of PABPC1 in gliomas with utilization of CGGA database and TCGA database, has detected a downregulated expression of PABPC1 in gliomas with higher malignance and high expression in procedural subtype, so it hinted the beneficial effect of PABPC1 in gliomas patients.

Interactions between the PABPC1 protein with BTG1 and BTG2 conserved motif can stimulate mRNA deadenylation

Directly binding between BTG/Tob proteins with the CAF1 deadenylase subunit of the CCR4-NOT complex requires the boxA and boxB, the two conserved motifs characteristic of the DTG/Tob APRO domain. In consistent with this fact, mRNA deadenylation and decay stimulated by those proteins can be seen in several instances. Among those members in the family, BTG1 and BTG2 were found to be associated with the protein arginine methyltransferase PRMT1 by the conserved motif, boxC, which is located in this subset of proteins. The nuclear magnetic resonance experiments and the biochemical analyses demonstrated that BTG1 and BTG2 can also contact the first RRM domain of the cytoplasmic poly(A) binding protein PABPC1. Deadenylation activated by BTG1 and BTG2 endowed by the process of PABPC1 mediated molecular interface is recently found to be a necessity for the T-cell quiescence maintenance.

Figure 1. The illustration of MKRN3-PABPC1 axis in the cell proliferation process of lung cancer (Wang et al., 2021).

References:

Wang Q, Wang Z, Bao Z, et al. PABPC1 relevant bioinformatic profiling and prognostic value in gliomas. Future Oncology, 2020, 16(01): 4279-4288.
Amine H, Ripin N, Sharma S, et al. A conserved motif in human BTG1 and BTG2 proteins mediates interaction with the poly (A) binding protein PABPC1 to stimulate mRNA deadenylation. RNA biology, 2021: 1-16.
Li K, Zheng X, Tang H, et al. E3 ligase MKRN3 is a tumor suppressor regulating PABPC1 ubiquitination in non–small cell lung cancer. Journal of Experimental Medicine, 2021, 218(8): e20210151.

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