Anna Maria Wawrzyniak

ORCID: 0000-0003-2911-9104
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About
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Research Areas
  • Cellular transport and secretion
  • Hippo pathway signaling and YAP/TAZ
  • Neurobiology and Insect Physiology Research
  • Lipid Membrane Structure and Behavior
  • Protein Kinase Regulation and GTPase Signaling
  • Autophagy in Disease and Therapy
  • Lysosomal Storage Disorders Research
  • Axon Guidance and Neuronal Signaling
  • Wnt/β-catenin signaling in development and cancer
  • Endoplasmic Reticulum Stress and Disease
  • Calcium signaling and nucleotide metabolism

Leibniz-Forschungsinstitut für Molekulare Pharmakologie
2021-2022

KU Leuven
2011-2020

Abstract Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, metabolites. Recruitment tethers to endoplasmic reticulum (ER) plasma is often triggered by calcium. Here we reveal a function for calcium in repression cholesterol export at ER Golgi complex. We show that efflux from stores induced inositol-triphosphate [IP 3 ] accumulation upon loss inositol 5-phosphatase INPP5A or receptor signaling triggers depletion associated Gb3 cell...

10.1038/s41467-021-22882-x article EN cc-by Nature Communications 2021-05-11

Abstract PDZ domain-containing proteins work as intracellular scaffolds to control spatio-temporal aspects of cell signalling. This function is supported by the ability their domains bind other such receptors, but also phosphoinositide lipids important for membrane trafficking. Here we report a crystal structure syntenin tandem in complex with carboxy-terminal fragment Frizzled 7 and phosphatidylinositol 4,5-bisphosphate (PIP 2 ). The reveals tripartite interaction formed via second domain...

10.1038/ncomms12101 article EN cc-by Nature Communications 2016-07-08

Syntenin-1 is a PDZ protein involved in receptor recycling and clustering. Its two domains interact with various receptors phosphoinositides, are flanked by N- C-terminal regions. Here, we report the identification of an autoinhibitory peptide stretch N-terminus that might be regulated phosphorylation. We further establish basic residues region mediate electrostatic interactions reconstituted liposomes contribute to plasma membrane targeting. Our study adds new components multi-dentate...

10.1016/j.febslet.2012.04.024 article EN FEBS Letters 2012-04-21

Background PDZ domains are highly abundant protein-protein interaction modules involved in the wiring of protein networks. Emerging evidence indicates that some also interact with phosphoinositides (PtdInsPs), important regulators cell polarization and signaling. Yet our knowledge on prevalence, specificity, affinity, molecular determinants PDZ-PtdInsPs interactions their impact PDZ-protein is very limited. Methodology/Principal Findings We screened human proteome for PtdInsPs interacting by...

10.1371/journal.pone.0054581 article EN cc-by PLoS ONE 2013-02-04

Lysosomes serve as dynamic regulators of cell and organismal physiology by integrating the degradation macromolecules with receptor nutrient signaling. Previous studies have established that activation transcription factor EB (TFEB) E3 (TFE3) induces expression lysosomal genes proteins in signaling-inactive starved cells, is, under conditions when activity master regulator nutrient-sensing signaling mechanistic target rapamycin complex 1 is repressed. How lysosome biogenesis triggered...

10.1016/j.jbc.2022.101740 article EN cc-by Journal of Biological Chemistry 2022-02-16

<title>Abstract</title> Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, metabolites. Recruitment tethers to endoplasmic reticulum (ER) plasma is often triggered by calcium. In contrast, we reveal here a function for calcium in repression cholesterol export at ER Golgi complex. We show that efflux from stores induced inositol-triphosphate [IP3] accumulation upon loss inositol 5-phosphatase INPP5A or sustained receptor signaling triggers...

10.21203/rs.3.rs-35925/v1 preprint EN cc-by Research Square (Research Square) 2020-07-16
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