Introduction and Gene Identity: The human TMA16 gene (Translation Machinery Associated 16, UniProt Q96EY4) encodes a small, 203-amino-acid protein that is conserved across eukaryotes (pmc.ncbi.nlm.nih.gov). It was originally identified in yeast (S. cerevisiae) as an uncharacterized protein associated with ribosomes (pmc.ncbi.nlm.nih.gov) and is also known by aliases such as C4orf43 (chromosome 4 open reading frame 43) and UPF0534 protein C4orf43 (www.genecards.org). TMA16 belongs to a eukaryote-specific protein family (Pfam PF11176) and has no bacterial homologs, indicating it evolved to assist the complex process of eukaryotic ribosome assembly. Importantly, TMA16 is not a ribosomal protein itself; rather, it functions as a ribosome assembly factor – one of the ~200 trans-acting factors that bind pre-ribosomal particles during maturation but do not become part of the final ribosome (pmc.ncbi.nlm.nih.gov). According to curated database annotations, TMA16 “enables preribosome binding activity” and is involved in 60S ribosomal subunit biogenesis, operating within the cell nucleus (localized to the nucleolus and nucleoplasm) (www.ncbi.nlm.nih.gov). In brief, TMA16 is a trans-acting helper protein required for building the large ribosomal subunit in human cells (www.genecards.org).
Role in 60S Ribosomal Subunit Biogenesis: Current understanding places TMA16 as a late-acting assembly factor that facilitates the maturation and nuclear export of the 60S subunit (the large subunit of the human ribosome). The 60S subunit contains the 5S, 5.8S, and 28S rRNAs and ~47 ribosomal proteins, and its assembly in the nucleus is a stepwise process requiring many helper proteins. TMA16’s primary function is to bind to immature 60S particles (pre-60S ribosomes) and aid their final maturation. A Swiss-Prot summary for human TMA16 notes that it is “involved in the biogenesis of the 60S ribosomal subunit in the nucleus” (www.genecards.org). More specifically, TMA16 appears to act by physically attaching to the pre-ribosome and stabilizing critical rRNA structures during the late stages of assembly. This is supported by gene ontology annotations that TMA16 binds preribosomal complexes and by its experimentally observed location on nascent 60S particles (www.ncbi.nlm.nih.gov).
Structural Insights (Cryo-EM Studies 2020–2023): Until recently, TMA16 was poorly characterized. However, breakthrough cryo-electron microscopy (cryo-EM) studies in the last few years have visualized TMA16 directly on assembling human ribosomes, revealing its location and interactions at near-atomic detail. A 2020 study in Nature Communications examined structures of human pre-60S particles and discovered a previously unknown factor bound to them; this factor was identified as TMA16 (pmc.ncbi.nlm.nih.gov). In those cryo-EM maps, TMA16 is seen wedged between the 5S ribonucleoprotein (5S RNP) (a complex of the 5S rRNA with ribosomal proteins L5 and L11 in the large subunit’s “central protuberance”) and the P0 stalk base of the large subunit (pmc.ncbi.nlm.nih.gov). In other words, TMA16 sits in a pocket on the pre-60S particle, occupying the space between the rotated 5S rRNA and the base of ribosomal protein P0 (which anchors the stalk that binds translation factors) (pmc.ncbi.nlm.nih.gov).
Identification of TMA16 in these structures was confirmed by cross-linking mass spectrometry (CXMS) evidence: the cryo-EM study reported a cross-link between lysine 114 of TMA16 and lysine 136 of ribosomal protein L18a (uL18) (pmc.ncbi.nlm.nih.gov), a physical contact that could only occur if the mystery protein was positioned on the pre-60S. This cross-link, together with the protein’s size and shape in the density map, allowed researchers to assign the density to TMA16 (pmc.ncbi.nlm.nih.gov). They built an atomic model for TMA16 (residues 17–166 of the 203 aa chain were resolved) bound to the pre-60S (pmc.ncbi.nlm.nih.gov). The model revealed that TMA16 is largely α-helical and uses an extended N-terminal helix to engage the ribosome. Notably, a long N-terminal helix (residues ~19–60) of TMA16 protrudes into the pre-60S particle, reaching ~60 Å in length (pmc.ncbi.nlm.nih.gov). This helix inserts alongside the rRNA and makes multiple contacts: researchers observed that conserved basic residues on TMA16 directly contact ribosomal RNA nucleotides (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For example, Histidine 18 and Arginine 22 of TMA16 form specific interactions with bases A1867 and G1864 in helix 39 of the 28S rRNA (pmc.ncbi.nlm.nih.gov). At the same time, the TMA16 helix is positioned against the 5S rRNA, interacting via several positively charged residues (pmc.ncbi.nlm.nih.gov). These multi-point contacts underscore TMA16’s role as an rRNA-binding assembly factor or “rRNA chaperone.” By binding simultaneously to the 5S rRNA and a region of the 28S rRNA (helix 39 and nearby helices), TMA16 bridges different parts of the ribosome. Its positioning was seen to cause a slight distortion (a deflection of a few Ångströms) in helix 39 of the rRNA – essentially TMA16 wedges into the particle and stabilizes a particular rRNA conformation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This is significant because during 60S maturation, the 5S RNP must rotate into its final position and several rRNA helices (like H39, H42, etc.) undergo remodeling; TMA16 appears to sense and perhaps promote the correct conformational changes in this region (pmc.ncbi.nlm.nih.gov).
Crucially, TMA16’s strategic location and contacts suggest a role in preparing the pre-60S for nuclear export. In the 2020 cryo-EM structures, TMA16 is present in “late nuclear” ribosome assembly intermediates – specifically, particles just after the loading of the essential export adapter NMD3 (which binds pre-60S to facilitate export) (pmc.ncbi.nlm.nih.gov). TMA16 itself does not appear in earlier-state particles, but only after the 5S RNP has rotated into place and NMD3 and the GTP-binding protein GTPBP4 (human homolog of yeast Nog1) are bound (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Given this timing, the authors proposed that TMA16 may function as an additional nuclear export factor or adapter that helps stabilize the pre-60S particle for transport to the cytoplasm (pmc.ncbi.nlm.nih.gov). The idea is that TMA16, by bridging the 5S RNP and nearby rRNA, might lock the structure in a state compatible with export through the nuclear pore. Supporting this notion, proteomic studies have found TMA16 in complex with known 60S export machinery. For example, a 2015 deep proteomics survey of CRM1 (XPO1) cargoes identified TMA16 among the proteins that interact with the Crm1 export pathway (pmc.ncbi.nlm.nih.gov). (Crm1 is the export receptor that recognizes NMD3; TMA16’s association with Crm1-containing complexes suggests it hitches a ride or contributes to the export of pre-60S subunits.)
Function and Interactions in the Assembly Pathway: TMA16 can be viewed as a late-stage 60S assembly factor that transiently binds pre-ribosomes and is released once its job is done. Its binding must be precisely timed within the assembly pathway. Structural analyses indicate that TMA16’s binding site on the pre-60S overlaps or clashes with some earlier assembly factors, meaning those factors must disassemble before TMA16 can bind (pmc.ncbi.nlm.nih.gov). Indeed, a recent 2023 study (Cell Research, 2023) that visualized even later nuclear assembly states found that TMA16 only appears after factors like NLE1 and CCDC86 have left the particle (pmc.ncbi.nlm.nih.gov). TMA16 also shares part of its binding region with NMD3 (the major export adaptor), implying a coordinated handoff or co-occupation: the late pre-60S can accommodate NMD3 together with TMA16, but as maturation proceeds, these factors will depart in sequence (pmc.ncbi.nlm.nih.gov). Once the pre-60S is ready for export and subsequent cytoplasmic maturation, TMA16 itself must be released – its position is incompatible with certain final remodeling events, so it cannot remain bound indefinitely (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
Experimental evidence confirms that TMA16’s attachment to pre-ribosomes is temporary and tightly regulated. In the cryo-EM series, TMA16 was present in specific intermediate states (“State A” in the 2020 study) but was absent from more mature states (States B and C) (pmc.ncbi.nlm.nih.gov), indicating it naturally dissociates as the particle matures. Moreover, blocking upstream steps causes TMA16 to accumulate aberrantly, highlighting its normal point of action. In yeast, for example, if the release of an upstream factor (Nog1, a GTPase in an earlier step) is genetically impaired, the yeast Tma16 protein builds up on stalled pre-60S particles (pmc.ncbi.nlm.nih.gov). Normally, Nog1 (human GTPBP4) is removed from the nascent 60S by an ATPase Drg1, allowing later factors to bind; if Nog1 fails to come off, Tma16 cannot progress and remains stuck (pmc.ncbi.nlm.nih.gov). This observation (from recent yeast genetics research) supports a model where TMA16 acts after Nog1/GTPBP4 function and likely before the final large subunit export and cytoplasmic maturation steps.
Once the pre-60S is exported to the cytoplasm, any remaining assembly factors must be removed so the subunit can participate in translation. Yeast studies show that Tma16 interacts with Rei1, a cytoplasmic 60S maturation factor (pmc.ncbi.nlm.nih.gov). Rei1 is known to bind pre-60S particles in the cytoplasm and help release certain nuclear export factors (like the shuttling protein Arx1). Cross-linking data revealed Tma16’s N-terminus contacts Rei1, and simultaneously Tma16’s C-terminus contacts ribosomal protein uL18 on the 60S (pmc.ncbi.nlm.nih.gov). This positioning suggests that in cytoplasmic 60S intermediates, Rei1 may directly engage Tma16 to trigger its dissociation. Consistent with this, the abundance pattern of Tma16 during purification of assembly intermediates in yeast closely mirrored that of the Arx1–Alb1 complex, which is a known nuclear export factor complex for the 60S (pmc.ncbi.nlm.nih.gov). Tma16 was enriched in late 60S particles (including those bound by Arx1 and by Lsg1 – a cytoplasmic factor for final 60S tuning), but not in very early ones (pmc.ncbi.nlm.nih.gov). Researchers concluded that Tma16 joins the pre-60S in the nucleus together with (or just after) the Arx1/Alb1 loading, travels with the particle to the cytoplasm, and is then removed there (pmc.ncbi.nlm.nih.gov). In other words, TMA16 functions analogously to a shuttling maturation factor that escorts the subunit through the nuclear pore and then hands it off to cytoplasmic factors.
Complex Formation with L10K (C19orf53): One of the latest developments (2023) in understanding TMA16 came from an even higher-resolution look at human pre-60S particles. In a late-stage pre-60S structure, TMA16 was found to partner with another small protein called C19orf53, also known as L10K (Leydig cell tumor 10 kDa protein homolog) (pmc.ncbi.nlm.nih.gov). L10K was an uncharacterized factor (10 kDa in size) that co-occupies the pre-60S at the final steps of nuclear maturation. The cryo-EM data showed that L10K binds adjacent to TMA16, and the two form a tight complex on the ribosome surface (pmc.ncbi.nlm.nih.gov). Specifically, L10K consists of a single helix with flexible loops, and this helix packs against TMA16’s helix in a hydrophobic interface (pmc.ncbi.nlm.nih.gov). The TMA16–L10K two-helix bundle encircles a segment of 28S rRNA (helix 89) in cooperation with GTPBP4 (pmc.ncbi.nlm.nih.gov). This three-factor cluster (TMA16, L10K, and GTPBP4) appears to clasp around rRNA helix 89, stabilizing it similarly to how another assembly factor (SDAD1) stabilizes a different rRNA helix in an earlier state (pmc.ncbi.nlm.nih.gov). The discovery of L10K partnering with TMA16 is a prime example of how multiple dedicated factors act together as rRNA chaperones: they locally confine and mold specific rRNA helices to ensure proper folding (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Importantly, the binding of TMA16/L10K requires that earlier factors (like NLE1 and CCDC86) have been released from the particle (pmc.ncbi.nlm.nih.gov). Once those are gone, TMA16 and L10K co-recruit to the site. Thus, TMA16 doesn’t act alone; it forms part of a late-assembly “checkpoint” complex with L10K (and likely GTPBP4 and others) that locks in the final rRNA architecture before the subunit is deemed export-competent (pmc.ncbi.nlm.nih.gov). This late complex is short-lived: after stabilizing the particle and facilitating the final rRNA arrangements, TMA16 and L10K both depart (neither is present in the fully mature 60S subunit). The coordinated release of these factors is one of the last steps before the large subunit joins the small subunit in the cytoplasm to form a functional ribosome.
Cellular Localization and Biochemical Pathway: In line with its role in ribosome biogenesis, TMA16 operates in the cell nucleus, where ribosomal subunits are assembled. High-throughput localization studies and curated annotations place TMA16 in the nucleolus (the site of rRNA transcription and early ribosome assembly) and the nucleoplasm (where later assembly steps occur) (www.ncbi.nlm.nih.gov). This distribution suggests TMA16 might shuttle or be present throughout the nucleus – possibly being recruited to pre-ribosomes as they transition from the nucleolus to nucleoplasm. Indeed, late 60S assembly (when TMA16 acts) typically occurs at the nucleoplasm/nuclear periphery, just before export. TMA16’s presence in the nucleolus could indicate it is synthesized and concentrated there, or that a fraction associates with particles still in nucleoli; however, its main functional engagement appears when pre-60S particles reach a more mature stage in the nucleoplasm. Consistent with being a ribosome assembly factor, TMA16 would be expected to colocalize with nucleolar/ribosomal markers and to leave the nucleus only bound to pre-60S particles. Once those particles export and shed their factors, TMA16 likely recycles back to the nucleus (similar to how NMD3 and other export factors shuttle back).
Biochemically, TMA16 is part of the ribosome assembly pathway, specifically the pathway of 60S subunit maturation. It does not act in isolation but interacts with numerous other assembly factors: for instance, as noted, it contacts GTPBP4 (Nog1), NMD3, Lsg1, Rei1, Arx1, ZNF593, and others in various stages (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov) (string-db.org). These interactions integrate TMA16 into the large network of ribosome biogenesis. Functionally, TMA16 doesn’t catalyze a chemical reaction (it is not an enzyme); rather, it serves a structural/regulatory role, ensuring that certain structural rearrangements in the pre-rRNA occur and that the pre-60S is competent for export. In terms of signaling pathways, ribosome assembly factors like TMA16 can be targets of cellular surveillance pathways – for example, if ribosome assembly fails (due to loss of TMA16 or others), cells activate a p53-dependent nucleolar stress response (pmc.ncbi.nlm.nih.gov). However, TMA16 itself is not known to be a signaling molecule; its role is confined to the biogenesis pathway of the ribosome, which is a fundamental biosynthetic process in the cell.
Evolutionary Conservation: The function of TMA16 appears to be ancient and conserved among eukaryotes. The very name “TMA16 homolog (S. cerevisiae)” in the human gene description highlights that yeast and human TMA16 are orthologs. Back in 2006, when the yeast protein Tma16 was first described, bioinformatics searches found putative TMA16 counterparts in insects, worms, plants, rodents, and humans (pmc.ncbi.nlm.nih.gov). Although the sequence similarity is modest (the short length and low complexity of the protein made E-values relatively high in those alignments), the presence of TMA16 across all these lineages suggests a conserved functional requirement (pmc.ncbi.nlm.nih.gov). Indeed, later experimental work has validated that yeast Tma16 and human TMA16 occupy equivalent positions on the pre-60S and likely perform analogous roles (pmc.ncbi.nlm.nih.gov). Key residues (like the aforementioned H18/R22 in human) are conserved in yeast, indicating that the rRNA-binding interface is under evolutionary constraint (pmc.ncbi.nlm.nih.gov). This conservation also extends to interactions: yeast Tma16 interacts genetically or physically with yeast Crm1 (exportin) and Rei1, just as human TMA16 interacts with XPO1 and has a presumed Rei1-like pathway (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The evolutionary retention of TMA16 in organisms from yeast to humans underscores that its role in ribosome biogenesis is fundamental. Not all ribosome assembly factors are universally conserved – some are specific to yeast or to metazoans – but TMA16 is one of those factors that appear to be present in all eukaryotes, implying the aspect of subunit maturation it participates in is a common, necessary step.
It is worth noting that TMA16 is an essential or vital gene in many contexts. In yeast, genome-wide studies have classified most ribosome biogenesis factors (including TMA16) as important for viability or optimal growth. While a yeast ∆tma16 deletion strain is viable in rich media (indicating Tma16 is not absolutely essential under standard conditions), it shows phenotypes under stress, and the cells grow more slowly (pmc.ncbi.nlm.nih.gov). In human cells, large-scale CRISPR/Cas9 knockout screens (such as those in the Cancer DepMap project) typically find that ribosome assembly factors are among the most critical genes for cell proliferation. Although specific CRISPR essentiality data for TMA16 were not detailed in literature, it can be inferred that loss of TMA16 would severely impair 60S production and cell growth, likely triggering p53-mediated apoptosis if p53 is intact (a common outcome of nucleolar disruption) (pmc.ncbi.nlm.nih.gov). This conjecture aligns with the fact that no inherited diseases have been reported for TMA16 mutations – a strong loss-of-function might be embryonic lethal, whereas milder variants have not yet been linked to a distinct disorder.
Biological and Medical Significance: Ribosome biogenesis is a process of keen interest in cell biology and medicine. Dysregulation of ribosome production is linked to disease: for example, a class of developmental disorders known as ribosomopathies are caused by mutations in ribosomal proteins or assembly factors (pmc.ncbi.nlm.nih.gov). Patients with ribosomopathies (such as Diamond-Blackfan anemia or Shwachman-Diamond syndrome) have defects in making ribosomes, leading to tissue-specific problems and a predisposition to cancer (pmc.ncbi.nlm.nih.gov). While no ribosomopathy is currently attributed to TMA16, this is possibly because TMA16 has not been found mutated in patient populations – it may be essential, as noted, or its mutations are very rare. Nonetheless, understanding TMA16’s function helps complete the picture of how large subunits are built, which is directly relevant to these diseases. For instance, if a patient had a mutation in TMA16 that reduces its function, one would predict a large subunit biogenesis defect (perhaps causing accumulation of unexported pre-60S in the nucleus, nucleolar stress, and downstream consequences). As genomic sequencing becomes more widespread, it is not implausible that future studies might identify individuals or cancer cells with TMA16 mutations, given the critical role of this protein.
In the context of cancer biology, ribosome biogenesis factors like TMA16 are gaining attention. Cancer cells typically ramp up ribosome production to support rapid growth, and in some cases they become “addicted” to this increased biogenesis. Evidence has emerged that dysfunctional ribosome assembly can contribute to oncogenesis or that cancer cells are selectively sensitive to perturbations in ribosome assembly (pmc.ncbi.nlm.nih.gov). A recent review by Pelletier et al. (2023) emphasizes that ribosome biogenesis and cancer are intimately connected, with many tumors showing overactive nucleoli and assembly factor dysregulation (pmc.ncbi.nlm.nih.gov). Consequently, targeting ribosome biogenesis is being explored as a therapeutic strategy (pmc.ncbi.nlm.nih.gov). Small-molecule inhibitors of rRNA synthesis (like CX-5461) or of nucleolar enzymes have entered clinical trials for cancer. Though there are no drugs targeting TMA16 specifically, one could conceptually consider that inhibiting a factor like TMA16 might slow 60S subunit production and thus protein synthesis in rapidly dividing cells. Any such approach would need to balance toxicity to normal cells, since ribosome assembly is essential in healthy tissues as well. However, the general principle is that certain assembly steps might be targetable “choke points” in cancer – and late-stage factors such as TMA16 could be of interest if tumor cells are more reliant on high ribosome output than normal cells.
From a research and “real-world” standpoint, the elucidation of TMA16’s role provides a new biomarker and potential handle for studying nucleolar stress. For example, the presence or absence of TMA16 on pre-ribosomes could be used experimentally to define the stage of ribosome assembly being affected by a drug or mutation. Its interactions (with GTPBP4, NMD3, L10K, etc.) form a network that can be probed to understand how assembly is coordinated. There are also biotechnological implications: proteins like TMA16, which bind specifically to pre-rRNA, could in theory be used to isolate late ribosome assembly intermediates or to develop assays for ribosome assembly activity in extracts. Indeed, the 2022 comprehensive study of 60S biogenesis factors used TMA16 as a handle (via epitope-tagging) to purify and analyze late 60S particles in yeast (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
In summary, TMA16 is a key player in the final stages of building the large ribosomal subunit. It acts within the nucleus to bind and stabilize the near-mature 60S precursors, working alongside other factors to ensure the subunit is correctly folded and ready for export. It then dissociates (likely in the cytoplasm) to allow completion of ribosome assembly. Discovered only in the last two decades and characterized in detail in the last few years, TMA16 has transitioned from a “gene of unknown function” to a well-defined 60S ribosome assembly factor. This knowledge deepens our fundamental understanding of ribosome biogenesis – a central process of life – and may inform medical research, as defects in ribosome assembly are linked to disease. Ongoing studies continue to investigate TMA16’s precise regulatory mechanisms (e.g. how its release is triggered, whether it is regulated by phosphorylation or other modifications) and to explore whether it has any moonlighting roles outside ribosome assembly (so far, none are known). Given its conservation and critical function, TMA16 exemplifies how even small, previously overlooked proteins can play outsized roles in the cell’s core machinery. In the current state of research (2023–2024), TMA16 is recognized as an essential facilitator of ribosomal large subunit formation, operating as part of a tightly coordinated assembly pathway with no known direct enzymatic activity but indispensable scaffold and checkpoint functions (www.genecards.org) (pmc.ncbi.nlm.nih.gov).
References:
Liang et al., Nature Communications, July 15, 2020. “Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.” (Cryo-EM study identifying TMA16 as a novel factor on late 60S; DOI: 10.1038/s41467-020-17237-x) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov)
Sailer et al., Cell Reports, Feb 8, 2022. “A comprehensive landscape of 60S ribosome biogenesis factors.” (Yeast study mapping assembly factor timing; confirms Tma16’s interactions with Rei1 and uL18 and its late joining of pre-60S; DOI: 10.1016/j.celrep.2022.110353) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov)
Ma et al. (Dong & Gao labs), Cell Research, July 25, 2023. “Visualizing the nucleoplasmic maturation of human pre-60S ribosomal particles.” (Higher-resolution cryo-EM of human 60S maturation; discovers TMA16–L10K complex encircling rRNA helix 89; DOI: 10.1038/s41422-023-00853-9) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov)
GeneCards/Human Genome/NCBI Gene (accessed 2025). TMA16 – Translation Machinery Associated 16 Homolog. (Database summary: “Enables preribosome binding activity. Involved in ribosomal large subunit biogenesis. Located in nucleolus and nucleoplasm.” – Alliance of Genome Resources, July 2025) (www.ncbi.nlm.nih.gov)
UniProt Knowledgebase (Swiss-Prot entry Q96EY4, last modified 2023). TMA16_HUMAN. (Protein entry: “Translation machinery-associated protein 16”; Function: involved in 60S ribosomal subunit biogenesis in the nucleus (www.genecards.org); notes protein family UPF0534 and synonyms C4orf43).
Fleischer et al., Genes & Development, May 15, 2006. “Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes.” (Yeast study that first named Tma16; shows conservation of TMA16 in eukaryotes (pmc.ncbi.nlm.nih.gov) and identified it in ribosome-bound fractions.)
Kirli et al., eLife, 2015. “A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.” (Proteomic study of export complexes; reported interactions linking TMA16 to CRM1 export pathway (pmc.ncbi.nlm.nih.gov)).
STRING protein network for human TMA16 (functional partners prediction, accessed 2024) – highlights high-confidence interactions with GTPBP4 (Nog1), NMD3, and other ribosome biogenesis factors (string-db.org).
Kressler et al., Seminars in Cell & Dev. Biology, 2017. “Factors associated with ribosome biogenesis” – Review (background: ~200 assembly factors assist ribosome assembly; general principles of RBF function) (pmc.ncbi.nlm.nih.gov).
Pelletier et al., Seminars in Cell & Dev. Biology, 2023. “Ribosome biogenesis in cancer: new players and therapeutic avenues.” (Review on links between ribosome assembly and cancer; discusses how perturbing biogenesis – potentially including factors like TMA16 – could be exploited in therapy) (pmc.ncbi.nlm.nih.gov).