Christoph Reiter

Mr. Christoph Reiter

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Research Focus & Metrics

Academic Career Length

2Years (2025-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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30 April 2026 in Preprints.org
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MSMehrta Shirzadian
Mehrta Shirzadian
EGEmanuel Gollob
Emanuel Gollob
CRChristoph Reiter
Christoph Reiter
URUlla Rauter
Ulla Rauter
MPManuel Paschinger
Manuel Paschinger
KSKlaus Spiess
Klaus Spiess
Human language continuously generates patterned mechanical vibrations, yet the cellular consequences of such structured sound remain largely unexplored. Here, we investigate whether acoustic vibration with different degrees of temporal and spectral organization modulates actin cable architecture and polarity in the non auditory eukaryote Saccharomyces cerevisiae. Using a direct contact stimulation setup, yeast cells expressing ABP140- GFP were exposed to sustained tonal sound, broadband white noise, or brief consonant like acoustic bursts designed to isolate speech relevant temporal structures without semantic content. Sustained tonal stimulation, characterized by rhythmic continuity and harmonic coherence similar to vowel like components of speech, increased ABP140- GFP signal intensity,actin branching and actin length and significantly enhanced shmoo formation. In contrast, broadband noise disrupted actin organization and suppressed shmooing, while transient consonant like bursts produced no measurable structural effects. These results indicate that language related acoustic structure, specifically sustained and coherent mechanical vibration, can modulate cytoskeletal organization in yeast, supporting the view of sound and speech as biologically active mechanical inputs rather than purely communicative signals.

23 June 2026 in Biomedicines
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GEGenevieve Edobor
Genevieve Edobor
RHRonald Thomas Huber
Ronald Thomas Huber
CRChristoph Reiter
Christoph Reiter
HGHanna Gercke
Hanna Gercke
NKNiklas Kaefer
Niklas Kaefer
HBHannelore BREITENBACH-KOLLER
Hannelore BREITENBACH-KOLLER
Across all kingdoms of life, ribosomes are indispensable molecular machines that translate genetic information into the proteome of living cells. The fundamental catalytic centers of the ribosome, constructed primarily from ribosomal RNA (rRNA), exhibit remarkable conservation between the major domains of life. The ribosome’s A-site deciphers the mRNA’s triplet code, while the P-site synthesizes the growing protein chain and the E-site provides exit for deacylated tRNA; a distinct tunnel facilitates nascent polypeptide export. While the conservation of ribosomal proteins is less pronounced between bacteria and eukaryotes, striking homology exists from simple eukaryotes to humans. Ribosomal proteins were traditionally viewed mainly as scaffolding agents, steering rRNA folding during ribosome biogenesis and maintaining structural stability during translation. However, since the early 2000s, advances in structural and functional ribosome analysis have ushered in a more nuanced paradigm: ribosomes are no longer considered uniform machines. Instead, an array of rRNA and ribosomal protein modifications generates a spectrum of ribosome populations capable of specialized translation. RiboScreenTM technology leverages this regulatory potential of individual ribosomal proteins, enabling deliberate modulation of target protein output and representing a promising tool for correcting dysregulated protein expression involved in rare and common diseases. This review will first introduce relevant aspects of ribosome biology and then showcase the tools of this new technology. Finally, we report examples for the delivery of small molecules to target ribosomal proteins for tailored restoration of protein production levels in rare and prevalent diseases.

11 July 2025 in bioRxiv
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MSMehrta Shirzadian
Mehrta Shirzadian
EGEmanuel Gollob
Emanuel Gollob
CRChristoph Reiter
Christoph Reiter
URUlla Rauter
Ulla Rauter
MPManuel Paschinger
Manuel Paschinger
KSKlaus Spiess
Klaus Spiess
What if vocal language were not only a medium for human communication but a vibrational force that leaves structural traces in living cells? This study explores how audible sound, particularly the structured elements of human speech, affects the cytoskeleton of Saccharomyces cerevisiae . Using a direct-contact acoustic system, we exposed yeast to distinct sound types: tonal vibrations, broadband noise, and consonant phonemes. Fluorescence microscopy revealed that tonal stimuli with coherent low-frequency patterns enhanced actin polymerization and shmoo formation, both markers of polarity and mating. In contrast, broadband noise disrupted actin integrity, while consonants produced no measurable effects. These results suggest that rhythmic continuity and spectral coherence, key features of speech, can modulate cytoskeletal organization in non-auditory cells. By reframing vocal language as mechanical input rather than semantic content, this study bridges microbial cell biology with acoustic ecology and proposes a new lens for exploring how human-generated soundscapes physically influence living systems.

2 November 2026 in The FEBS Journal
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CRChristoph Reiter
Christoph Reiter
PEPatrick Ebner
Patrick Ebner
EKElli Leona Kronsteiner
Elli Leona Kronsteiner
SMSophia Moustakakis
Sophia Moustakakis
MWMarkus Wiederstein
Markus Wiederstein
Mark RinnerthalerMark Rinnerthaler
Mark Rinnerthaler
Lipid droplets (LDs) are organelles found in all eukaryotic cells, yet their contribution toward proteostasis is still poorly understood. In this study, we demonstrate that LDs in the model organism Saccharomyces cerevisiae function as transporters to which cytosolic protein aggregates attach for transport to the vacuole for degradation. With the help of chaperones and the yeast prion Rnq1, serving as an aggregation model, and using techniques such as live‐cell imaging, super‐resolution microscopy, electron microscopy, and biochemical analyses, we demonstrate that protein aggregates bind to LDs, are transported through the cytoplasm, and are ultimately transferred to the insoluble protein deposit (IPOD) on the vacuole surface. The efficiency of this process is highly dependent on the lipid composition of the LDs, with triacylglycerols identified as key determinants for aggregate docking. In LD‐deficient cells, we observed severe fragmentation of the aggregates and a complete loss of IPOD, whereas stimulation of LD formation significantly increased the size of IPOD and vacuolar import activity. Overall, our results expand the understanding of cellular protein quality control and link lipid metabolism research to the regulation of protein aggregation. The evidence that LDs act as ‘garbage trucks’ transporting protein aggregates to the vacuole reveals a new interface between proteostasis and lipid metabolism that could also be significant in higher eukaryotes.