Abstract
ATP/GTP binding protein 1 (AGTPBP1) encodes a crucial protein, cytosolic carboxypeptidase 1 (CCP1), which plays a role in modulating the polyglutamylation of tubulin and has been studied in degenerative diseases. However, the role of AGTPBP1 in malignancy has not been completely studied yet. In this study, we examined the role of AGTPBP1 in cancer progression, its association with patient survival, and related mechanisms in lung cancer, using the A549 cell line and lung cancer gene expression datasets. AGTPBP1 knockdown increased the proliferation, migration, sphere formation, and drug resistance of A549 cells. Lung cancer datasets revealed significantly lower mRNA and protein expression levels of AGTPBP1 in lung cancer tissues, as compared to those in normal tissues. Importantly, AGTPBP1 expression positively correlated with patient survival. Analysis of co-expressed genes revealed that AGTPBP1 expression positively correlated with immune infiltration in lung cancer. Our results conclusively suggested that AGTPBP1 expression was correlated with cancer progression and immune infiltration in lung cancer.
Highlights
ATP/GTP binding protein 1 (AGTPBP1) encodes the protein, cytosolic carboxypeptidase 1 (CCP1), which mediates deglutamylation to maintain steady-state levels of polyglutamylated tubulin [1]
A distribution pattern of AGTPBP1 expression in diverse normal tissues obtained from Human Protein Atlas (HPA) [36] revealed that the mRNA expression level of AGTPBP1 was higher in lung tissue and in bone marrow, cerebral cortex, granulocytes, and testis, as compared to that in other tissues (Supplementary Figure S1)
SOX2 and NANOG were significantly upregulated in AGTPBP1-silenced A549 cells, as compared to control, whereas no differential expression of OCT4 and c-MYC was observed between AGTPBP1-silenced cells and control cells (Figure 1e)
Summary
ATP/GTP binding protein 1 (AGTPBP1) encodes the protein, cytosolic carboxypeptidase 1 (CCP1), which mediates deglutamylation to maintain steady-state levels of polyglutamylated tubulin [1]. It has been revealed that CCP1 catalyzes the removal of glutamate residues from both the polyglutamyl side chanins of α- and β-tubulin and detyrosinated α-tubulin and induces the polymerization of α-tubulin [1,7]. These molecular functions can maintain steady-state levels of polyglutamylated microtubules in neurons [8], axoneme [9], mitotic spindles [10], ciliary dynein [11], and basal bodies [12]. The role of AGTPBP1 in human malignancy has not been comprehensively studied yet
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