Iris K. Jarsch

ORCID: 0000-0003-3218-1742
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About
Contact & Profiles
Research Areas
  • Legume Nitrogen Fixing Symbiosis
  • Cellular Mechanics and Interactions
  • Lipid Membrane Structure and Behavior
  • Plant-Microbe Interactions and Immunity
  • Photosynthetic Processes and Mechanisms
  • Plant Molecular Biology Research
  • Cellular transport and secretion
  • RNA Research and Splicing
  • Plant Pathogenic Bacteria Studies
  • Signaling Pathways in Disease
  • Plant Reproductive Biology
  • Biochemical and Structural Characterization
  • RNA Interference and Gene Delivery
  • Cell Adhesion Molecules Research
  • Plant Stress Responses and Tolerance
  • Plant nutrient uptake and metabolism
  • Advanced Fluorescence Microscopy Techniques
  • Hippo pathway signaling and YAP/TAZ
  • Nuclear Structure and Function

University of Cambridge
2016-2021

The Gurdon Institute
2016-2021

Ludwig-Maximilians-Universität München
2010-2021

Urologische Klinik München
2010-2021

Wellcome Trust
2016-2017

Cell surface receptors govern a multitude of signalling pathways in multicellular organisms. In plants, prominent examples are the receptor kinases FLS2 and BRI1, which activate immunity steroid-mediated growth, respectively. Intriguingly, despite inducing distinct outputs, both employ common downstream components, exist plasma membrane (PM)-localised protein complexes. An important question is thus how these complexes maintain specificity. Live-cell imaging revealed that BRI1 form PM...

10.7554/elife.25114 article EN cc-by eLife 2017-03-06

Eukaryotic plasma membranes are highly compartmentalized structures. So far, only a few individual proteins that function in wide range of cellular processes have been shown to segregate into microdomains. However, the biological roles most microdomain-associated unknown. Here, we investigated heterogeneity distinct microdomains and complexity their coexistence. This diversity was determined living cells intact multicellular tissues using 20 different marker from Arabidopsis thaliana, mostly...

10.1105/tpc.114.124446 article EN The Plant Cell 2014-04-01

Summary Remorins are well‐established marker proteins for plasma membrane microdomains. They specifically localize to the inner leaflet despite an overall hydrophilic amino acid composition. Here, we determined acids and post‐translational lipidations that required association of remorin proteins. We used a combination cell biological biochemical approaches truncated variants those in living cells S‐acylation on defined residues these cysteine C‐terminal hydrophobic core contributes most...

10.1111/nph.12867 article EN New Phytologist 2014-06-04

Assemblies of actin and its regulators underlie the dynamic morphology all eukaryotic cells. To understand how regulatory proteins work together to generate actin-rich structures such as filopodia, we analyzed localization diverse within filopodia in Drosophila embryos a complementary vitro system filopodia-like (FLSs). We found that composition protein complex where is incorporated (the filopodial tip complex) remarkably heterogeneous both vivo vitro. Our data reveal different pairs...

10.1083/jcb.202003052 article EN cc-by The Journal of Cell Biology 2021-03-18

Abstract Plant growth and development are modulated by both biotic abiotic stress. Increasing evidence suggests that cellular integration of the corresponding signals occurs within preformed hubs at plasma membrane called nanodomains. These sub-compartments organized multivalent molecular scaffold proteins, such as remorins. Here, we demonstrate Group 1 remorins form a hetero-oligomeric complex membrane. While these functionally redundant for some pathways their multivalency also allows...

10.1101/2021.01.28.428596 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-01-29

Filopodia are finger-like actin-rich protrusions that extend from the cell surface and important for cell–cell communication pathogen internalization. The small size transient nature of filopodia combined with shared usage actin regulators within cells confounds attempts to identify filopodial proteins. Here, we used phage display phenotypic screening isolate antibodies alter morphology filopodia-like structures (FLS) in vitro. We found all cause shorter FLS interact SNX9, an regulator binds...

10.1083/jcb.201909178 article EN cc-by The Journal of Cell Biology 2020-03-25

Abstract Assemblies of actin and its regulators underlie the dynamic morphology all eukaryotic cells. To begin to understand how diverse regulatory proteins work together generate actin-rich structures we tracked assembly their relative proportions in a cell-free system that generates filopodia-like (FLS). We found heterogeneous mixtures could give rise morphologically similar FLS bundles exhibited simple behaviour growth shrinkage. explain these observations, combined experiment with...

10.1101/525725 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2019-01-23

Filopodia are finger-like actin-rich protrusions that extend from the cell surface and important for cell-cell communication pathogen internalization. The small size transient nature of filopodia combined with shared usage actin regulators within cells confounds attempts to identify filopodial proteins. Here, we used phage display phenotypic screening isolate antibodies alter morphology filopodia-like structures (FLS) in vitro. We found all cause shorter FLS interact SNX9, an regulator binds...

10.17863/cam.52814 article EN 2020-04-01
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