FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved in colorectal cancer progression. (March 2017)

• Record Type: Journal Article
• Authors: Akter, Khondker Ayesha; Mansour, Mohammed A.; Hyodo, Toshinori; Senga, Takeshi
• Is Part Of: International journal of biochemistry & cell biology. Volume 84(2017)
• Page Start: 1
• Page End: 13
• Publication Date: 2017-03
• Subjects: Colorectal cancer -- FAM98A -- FAM98B -- PRMT1; Biochemistry -- Periodicals; Cytology -- Periodicals; Biochemistry -- Periodicals; Cell Biology -- Periodicals; Biochimie -- Périodiques; Cytologie -- Périodiques; Biochimie; Cytologie; Biochemistry; Cytology; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); Periodicals; 572.05
• DOI: 10.1016/j.biocel.2016.12.013
• Languages: English
• ISSNs: 1357-2725

Abstract

Highlights: FAM98A is included in a complex with DDX1 and C14orf166. FAM98A and FAM98B are required for PRMT1 expression. Knockdown of FAM98A or FAM98B suppress CRC progression. Abstract: Protein Arginine Methyl Transferase 1 (PRMT1) is deemed to be a potential oncogenic protein considering its overexpression in several malignancies including colorectal cancer. However, the molecular pathogenesis regarding PRMT1 overexpression and overall poor patient survival involved in this devastating and life threatening cancer remains obscured. In our previous study, we have identified FAM98A as a novel substrate of PRMT1 and also identified its role in ovarian cancer progression. Here, we showed that the two structural homologs FAM98A and FAM98B included in a novel complex with DDX1 and C14orf166 are required for PRMT1 expression. Analysis of the data from The Cancer Genome Atlas (TCGA) database and clinical colorectal cancer specimens also demonstrated a strong positive correlation and co-occurrence of PRMT1, FAM98A and FAM98B. These findings provide a mechanistic insight into how knockdown of FAM98A or FAM98B can suppress the malignant characteristics of cancer cells. Besides, we showed that FAM98A and FAM98B are working in the same axis as knockdown of both proteins together does not cause additional reduction in the cellular proliferation and colony formation of colorectal cancer cells.