| 2016 |
FAM98A binds to PLEKHM1 and, together with NDEL1, connects lysosomes to microtubules. This PLEKHM1/DEF8/RAB7/FAM98A/NDEL1 complex regulates peripheral lysosome positioning and secretion in osteoclasts; knockdown of FAM98A phenocopies lysosome positioning and bone resorption defects seen in Plekhm1-null osteoclasts. |
Co-immunoprecipitation/interaction analysis, siRNA knockdown with lysosome distribution and bone resorption phenotypic readouts in osteoclasts |
JCI insight |
Medium |
27777970
|
| 2015 |
FAM98A is a substrate of PRMT1 (protein arginine methyltransferase 1); PRMT1 arginine-methylates FAM98A, and FAM98A is required for tumor cell migration, invasion, and colony formation in ovarian cancer cells. |
In vitro methylation assay (PRMT1 substrate screen), siRNA knockdown with migration/invasion/colony formation assays |
Tumour biology |
Medium |
26503212
|
| 2016 |
FAM98A and FAM98B form a complex with DDX1 and C14orf166 (DDX1-C14orf166-FAM98A/B complex); this complex is required for PRMT1 expression, and knockdown of FAM98A suppresses PRMT1 levels, proliferation, and colony formation in colorectal cancer cells. |
Co-immunoprecipitation, siRNA knockdown with proliferation and colony formation assays, TCGA correlation analysis |
The international journal of biochemistry & cell biology |
Medium |
28040436
|
| 2018 |
FAM98A localizes to stress granules (but not P-bodies) upon various stress stimuli; its C-terminal low-complexity region is required for this localization; FAM98A depletion reduces the number of stress granules per cell; FAM98A associates with stress granule proteins DDX1, ATXN2, ATXN2L, and NUFIP2. |
Fluorescence microscopy (live imaging/immunofluorescence), deletion mutant analysis, siRNA knockdown, co-immunoprecipitation |
Molecular and cellular biochemistry |
Medium |
29992460
|
| 2018 |
FAM98A overexpression activates the P38-ATF2 signaling pathway, increasing phospho-P38, phospho-ATF2, and cyclin D1 levels, thereby promoting lung cancer cell proliferation; a P38-specific inhibitor reverses FAM98A overexpression effects. |
Overexpression and siRNA knockdown in NSCLC cell lines, Western blotting for pathway components, pharmacological inhibition of P38 |
Cancer management and research |
Low |
30100758
|
| 2022 |
FAM98A promotes resistance to 5-fluorouracil in colorectal cancer cells by inhibiting ferroptosis through activation of xCT translation in stress granules. |
Overexpression/knockdown, immunoblotting, immunoprecipitation to identify FAM98A-SG association and xCT pathway activation, in vitro and in vivo proliferation assays |
Archives of biochemistry and biophysics |
Low |
35421356
|
| 2023 |
Five novel arginine dimethylation sites on FAM98A were identified by targeted proteomics; dimethylation-deficient mutation of FAM98A suppressed cell migration to the same extent as FAM98A deletion, indicating that PRMT1-mediated dimethylation of these sites mediates FAM98A's role in cell migration. |
Metabolic stable-isotope labeling (mNeuCode), targeted MS/MS, site-directed mutagenesis of dimethylation sites, cell migration assay in FAM98A-KO HeLa cells |
Analytical chemistry |
Medium |
36757215
|
| 2025 |
FAM98A assembles with RTCB (the catalytic tRNA ligase subunit) and other subunits into a compositionally distinct tRNA ligase complex that lacks Ashwin, distinguishing it from the FAM98B-containing nuclear complex; cryo-EM structure of the tRNA-LC shows FAM98B (the paralog) forms an intricately co-folded heterodimer with CGI-99 that clamps Ashwin, providing a structural rationale for why FAM98A- and FAM98C-containing complexes lack Ashwin and may have distinct cellular functions. |
Cryo-EM (atomic-resolution reconstruction), structure-based mutagenesis, interaction analysis of tRNA-LC subunits |
bioRxiv (preprint)preprint |
High |
bio_10.1101_2025.08.01.668197
|
| 2025 |
FAM98A defines one of three compositionally distinct RTCB-containing tRNA ligase complex forms (FAM98A-, FAM98B-, or FAM98C-containing); FAM98A-containing complexes lack Ashwin (the nuclear import factor), so FAM98A-associated complexes are retained in the cytoplasm rather than being imported to the nucleus, establishing FAM98A as a determinant of cytoplasmic tRNA-LC localization. |
Biochemical fractionation, interaction assays, NLS disruption/rescue experiments, pre-tRNA splicing assays |
bioRxiv (preprint)preprint |
High |
bio_10.1101_2025.08.01.668163
|
| 2025 |
Conditional knockout of Fam98a in myeloid osteoclast precursors does not reduce trabecular or cortical bone mass in mice, nor does it impair osteoclastogenesis or bone resorption in vitro, apparently because Fam98b expression is upregulated to compensate; in contrast, knockdown of Fam98b in osteoclasts disrupts lysosome trafficking and bone resorption with phenotypes similar to Fam98a knockdown (negative result for in vivo FAM98A loss-of-function). |
Myeloid-specific conditional Fam98a knockout mice, shRNA knockdown, osteoclastogenesis assays, bone resorption assays, micro-CT bone mass measurement |
Biology |
Medium |
39857276
|