Lisa Larsson Berglund

ORCID: 0000-0001-6704-1876
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About
Contact & Profiles
Research Areas
  • Fungal and yeast genetics research
  • Heat shock proteins research
  • Endoplasmic Reticulum Stress and Disease
  • Genetic Neurodegenerative Diseases
  • Genetics, Aging, and Longevity in Model Organisms
  • DNA Repair Mechanisms
  • Cellular transport and secretion
  • Calpain Protease Function and Regulation
  • Nuclear Structure and Function
  • Cardiomyopathy and Myosin Studies

University of Gothenburg
2017-2024

Significance A defining feature of eukaryotes is the nuclear envelope, a double lipid bilayer that serves to isolate and protect cell’s genetic material. Transport large molecules over this barrier believed occur almost exclusively via pores. However, herpes virions mega-ribonucleoproteins (megaRNPs) use an alternative means transport—via envelope budding (NEB). Here, we show NEB ubiquitous eukaryotic phenomenon increases when exposed various forms cellular stress. frequency was maximal cell...

10.1073/pnas.2020997118 article EN cc-by Proceedings of the National Academy of Sciences 2021-07-21

Abstract The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic biosynthesis system. Here, we find age-associated metabolic cues target yeast disaggregase Hsp104 to maintain functional nuclear proteome during quiescence. switch respiratory metabolism accompanying decrease in translation rates direct interact latent...

10.1038/s41467-023-44538-8 article EN cc-by Nature Communications 2024-01-05

In this paper, we show that the essential Hsp90 co-chaperone Sgt1 is a member of general protein quality control network links folding and degradation through its participation in misfolded proteins both cytosol endoplasmic reticulum (ER). Sgt1-dependent acts parallel pathway to ubiquitin ligase (E3) chain elongase (E4), Hul5, overproduction Hul5 partly suppresses defects cells with reduced activity. Upon proteostatic stress, accumulates transiently, an Hsp90- proteasome-dependent manner,...

10.1016/j.celrep.2021.109328 article EN cc-by Cell Reports 2021-06-01

Membrane contact sites facilitate the exchange of metabolites between organelles to support interorganellar communication. The nucleus-vacuole junctions (NVJs) establish physical perinuclear endoplasmic reticulum (ER) and vacuole. Although NVJ tethers are known, how abundance composition controlled in response metabolic cues remains elusive. Here, we identify ER protein Snd3 as central factor for formation. interacts with tethers, supports their targeting contacts, is essential Upon glucose...

10.1016/j.celrep.2020.108637 article EN cc-by Cell Reports 2021-01-01

ABSTRACT When the temperature is increased, heat-shock response activated to protect cellular environment. The transcriptomics and proteomics of this process are intensively studied, while information about how cell responds structurally heat stress mostly lacking. Here, Saccharomyces cerevisiae were subjected a mild continuous shock (38°C) intermittently cryo-immobilised for electron microscopy. Through measuring changes in all distinguishable organelle numbers, sizes morphologies over 2100...

10.1242/jcs.258325 article EN cc-by Journal of Cell Science 2021-07-07

A major consequence of aging and stress, in yeast to humans, is an increased accumulation protein aggregates at distinct sites within the cells. Using genetic screens, immunoelectron microscopy, three-dimensional modeling our efforts elucidate importance aggregate annexation, we found that most accumulate near surface mitochondria. Further, show virus-like particles (VLPs), which are part retrotransposition cycle Ty elements, markedly enriched these aggregation. RNA interference-mediated...

10.1073/pnas.2313538121 article EN cc-by Proceedings of the National Academy of Sciences 2024-03-25

The accumulation of misfolded proteins is a hallmark aging and many neurodegenerative diseases, making it important to understand how the cellular machinery recognizes processes such proteins. A key question in this respect whether are handled similar way regardless their genetic origin. To approach question, we compared three different proteins, guk1-7, gus1-3, pro3-1, by cell. We show that all nontoxic, even though highly overexpressed, highlighting usefulness analyzing response misfolding...

10.1016/j.jbc.2022.102476 article EN cc-by Journal of Biological Chemistry 2022-09-09

Abstract Huntington’s disease develops when the polyglutamine (polyQ) repeat in Huntingtin (Htt) protein is expanded to over 35 glutamines rendering it aggregation-prone. Here, using Htt exon-1 as a polyQ model genome-wide screen yeast, we show that normal and soluble toxic cells with defects type-1 myosin-dependent endocytosis. The toxicity of linked physical interactions myosins, which occur via proline-rich region, leading reduction actin patch polarization clathrin-dependent An expansion...

10.1038/s41598-017-11102-6 article EN cc-by Scientific Reports 2017-09-06

Abstract When the temperature is increased, heat shock response activated to protect cellular environment. The transcriptomics and proteomics of this process are intensively studied, while information about how cell responds structurally stress mostly lacking. Here, Saccharomyces cerevisiae were subjected a mild continuous intermittently cryo-immobilized for electron microscopy. Through measuring changes in all distinguishable organelle numbers, sizes, morphologies over 2400 micrographs...

10.1101/2021.01.25.428102 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-01-26
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