Gunter B. Sissoko

ORCID: 0000-0003-4665-9305
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About
Contact & Profiles
Research Areas
  • Microtubule and mitosis dynamics
  • Cellular transport and secretion
  • CRISPR and Genetic Engineering
  • Genomics and Chromatin Dynamics
  • RNA regulation and disease
  • Ubiquitin and proteasome pathways
  • Circadian rhythm and melatonin
  • Photosynthetic Processes and Mechanisms
  • Protein Structure and Dynamics
  • Sleep and Wakefulness Research
  • RNA Research and Splicing
  • Nuclear Structure and Function
  • RNA and protein synthesis mechanisms
  • Neurobiology and Insect Physiology Research

Massachusetts Institute of Technology
2023-2024

Whitehead Institute for Biomedical Research
2023-2024

Columbia University
2018

Although sleep appears to be broadly conserved in animals, the physiological functions of remain unclear. In this study, we sought identify a defect common diverse group short-sleeping Drosophila mutants, which might provide insight into function and regulation sleep. We found that these mutants share phenotype sensitivity acute oxidative stress, exhibiting shorter survival times than controls. further showed increasing wild-type flies using genetic or pharmacological approaches increases...

10.1371/journal.pbio.2005206 article EN cc-by PLoS Biology 2018-07-12

Regulated start-codon selection has the potential to reshape proteome through differential production of uORFs, canonical proteins, and alternative translational isoforms. However, conditions under which is altered remain poorly defined. Here, using transcriptome-wide translation initiation site profiling, we reveal a global increase in stringency during mammalian mitosis. Low-efficiency sites are preferentially repressed mitosis, resulting pervasive changes thousands start their...

10.1101/2024.04.06.588385 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-04-06

Summary To faithfully segregate chromosomes during vertebrate mitosis, kinetochore-microtubule interactions must be restricted to a single site on each chromosome. Prior work pair-wise kinetochore protein has been unable identify the mechanisms that prevent formation in regions with low density of CENP-A nucleosomes. investigate impact higher-order assembly formation, we generated defined oligomers inner CENP-T using two distinct, genetically engineered systems human cells. Although...

10.1101/2023.05.22.541649 preprint EN cc-by-nc bioRxiv (Cold Spring Harbor Laboratory) 2023-05-22

Macromolecular assembly depends on tightly regulated pairwise binding interactions that are selectively favored at sites while being disfavored in the soluble phase. This selective control can arise due to molecular density-enhanced binding, as recently found for kinetochore scaffold protein CENP-T. When clustered, CENP-T recruits markedly more Ndc80 complexes than its monomeric counterpart, but underlying basis remains elusive. Here, we use quantitative

10.1101/2024.02.25.581584 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-02-26

Macromolecular assembly depends on tightly regulated pairwise binding interactions that are selectively favored at sites while being disfavored in the soluble phase. This selective control can arise due to molecular density-enhanced binding, as recently found for kinetochore scaffold protein CENP-T. When clustered, CENP-T recruits markedly more Ndc80 complexes than its monomeric counterpart, but underlying basis remains elusive. Here, we use quantitative vitro assays reveal two distinct...

10.1073/pnas.2401344121 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2024-12-19
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