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Hellström-Lindberg, E.

Publications and source records attributed to Hellström-Lindberg, E..

3 recordsLinked to original sources

Proteomics of steady-state and culture-derived human erythropoiesis reveals the dynamics of erythroid stress

To generate a mature red blood cell, erythropoiesis requires the committed erythroid progenitor cell and later erythroblast stages to undergo a continuum of extreme morphological and functional remodeling. In vitro culture has been crucial to understand the extensive proteome dynamics that underlie this process. However, the millions of cells required for conventional proteomics technologies preclude the study of erythropoiesis within the steady-state human bone marrow (BM). Thus, culture-induced stress may shape our understanding of erythroid maturation. To address this knowledge gap, we developed an optimized methodology for low-cell proteomics (pauciproteomics) and pursued total proteomic analysis of paired steady-state BM and culture-derived erythroid precursor stages from 11 healthy donors. This approach defines four main protein expression patterns during BM erythroid maturation which are only partially recapitulated by cultured cells. Culture-induced stress rewires the erythroid proteome from early stages of differentiation, reshaping major transcription factor networks, kinase pathways, metabolic enzymes and erythrokine regulation. Notably, single-cell RNA sequencing analysis of steady-state healthy and myelodysplastic syndromes (MDS) BM demonstrates that the cultured cell proteome parallels gene expression dynamics within the MDS BM, modelling the regulation of in vivo stress erythropoiesis. Culture-specific alterations were mostly restricted to extensive carbonic anhydrase dysregulation and embryofetal globin switching, both potentially linked to altered gas exchange dynamics in culture. In conclusion, we reveal the steady-state erythroid proteome and its substantial remodeling by culture-induced stress, reframing existing knowledge on erythroid differentiation, defining new elements of stress erythropoiesis and guiding future studies in the field.

physiology↗

RNA splicing factor mutations drive myeloid neoplasm oncogenesis through protein complex poisoning

RNA splicing factor mutations (SFmut) are founding oncogenic events which cause RNA splicing errors with unpredictable gene expression dynamics. Despite extensive transcriptomic studies, SFmut cancer-initiating mechanisms remain elusive. Among SFmut cancers, myeloid neoplasms (MN) alone offer a setting where true cancer-driving SFmut stem cells can be identified, namely the hematopoietic stem cell (HSC). Within a cohort of 62 MN patients and 20 healthy donors, we conducted long/short-read single-cell transcriptomics (10X-ONT, n = 21) and immunophenotype-resolved low-cell proteomics (pauciproteomics, n = 78) to resolve gene expression, RNA splicing and protein expression dynamics across healthy and SFmut MN hematopoiesis. During hematopoietic differentiation, SFmut RNA mis-splicing decouples proteotranscriptomic dynamics in a mutation-specific manner. Pauciproteomics defines the functional effects of SFmut RNA mis-splicing on the protein layer, identifying early-stage protein effects which poison entire functional protein complexes and progressively disrupt the proteome-wide network during cellular maturation. Importantly, this information could neither be resolved nor predicted by transcriptomic analyses. Finally, we functionally validate the proteome dynamics of HSC through induced pluripotent stem cell culture models of early hematopoietic differentiation, identifying candidate mechanisms for SFmut oncogenesis. Overall, these data elucidate SFmut MN disease biology with unprecedented granularity, defining the molecular consequences of SFmut RNA mis-splicing and offering a generalizable framework for cancer stem cell studies.

cancer biology↗

SF3B1-mutant mis-splicing of UBA1 confers a targetable therapeutic vulnerability through UBA1 inhibition

SF3B1 mutation-driven myelodysplastic syndromes (MDS-SF3B1) arise due to somatic mutation in the splicing factor SF3B1 gene. SF3B1 mutations induce RNA mis-splicing and loss of expression of critical genes for erythropoiesis, leading to erythroid dysplasia and ultimately refractory anemia. The development of precision medicine approaches for MDS- SF3B1 is hampered by the complexity of the mis-splicing landscape and its evaluation in disease-accurate model systems. To identify novel RNA mis-splicing events, isogenic SF3B1K700E and SF3B1WT iPSC lines from an MDS-SF3B1 patient were differentiated into hematopoietic cells in vitro and subjected to unsupervised splicing event analysis using full-length RNA sequencing data. This revealed SF3B1K700E-specific mis-splicing of ubiquitin-like modifier activating enzyme 1 (UBA1) transcripts, which encode the essential E1 protein at the apex of the ubiquitination cascade. UBA1 mis-splicing (UBA1ms) preserved UBA1ms mRNA but not protein expression. Consequently, UBA1ms diminished the pool of functional UBA1, sensitizing SF3B1K700E cell lines to the small-molecule UBA1 inhibitor TAK-243. Finally, analysis of CD34+ RNA sequencing data from an MDS patient cohort confirmed unique and ubiquitous UBA1ms in MDS-SF3B1 patients, without detection in other splicing factor-mutated MDS patients, or in healthy individuals. TAK-243 selectively targeted MDS-SF3B1 primary CD34+ cells and reduced mutant cell number in colony-forming unit studies. In contrast, normal hematopoietic progenitor cells were unaffected. Altogether, we here define UBA1ms as a novel therapeutic vulnerability in SF3B1-mutant cells, introducing UBA1 inhibition as a potential avenue for future MDS-SF3B1 treatments.

cancer biology↗