Agnieszka Biernatowska

ORCID: 0000-0002-7028-8412
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About
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Research Areas
  • Caveolin-1 and cellular processes
  • Erythrocyte Function and Pathophysiology
  • Lipid Membrane Structure and Behavior
  • Blood properties and coagulation
  • Cellular transport and secretion
  • Protein Kinase Regulation and GTPase Signaling
  • Endoplasmic Reticulum Stress and Disease
  • Trace Elements in Health
  • Cancer therapeutics and mechanisms
  • Pancreatic function and diabetes
  • Wnt/β-catenin signaling in development and cancer
  • Signaling Pathways in Disease
  • Phagocytosis and Immune Regulation
  • Sphingolipid Metabolism and Signaling
  • Lipid metabolism and disorders
  • Hippo pathway signaling and YAP/TAZ
  • Nanopore and Nanochannel Transport Studies
  • Lipid metabolism and biosynthesis
  • Peroxisome Proliferator-Activated Receptors
  • Lung Cancer Research Studies
  • RNA Interference and Gene Delivery
  • Cancer Mechanisms and Therapy
  • RNA and protein synthesis mechanisms

University of Wrocław
2013-2025

A plethora of novel information has emerged over the past decade regarding protein lipidation. The reversible attachment palmitic acid to cysteine residues, termed S-palmitoylation, focused a special attention. This is mainly due unique role this modification in regulation trafficking and function. large family acyltransferases (PATs) containing conserved aspartate–histidine–histidine–cysteine motif use ping-pong kinetic mechanism catalyze S-palmitoylation substrate protein. Here, we discuss...

10.1177/1535370217707732 article EN Experimental Biology and Medicine 2017-05-09

The existence of membrane-rafts helps to conceptually understand the spatiotemporal organization membrane-associated events (signaling, fusion, fission, etc.). However, as rafts themselves are nanoscopic, dynamic, and transient assemblies, they cannot be directly observed in a metabolizing cell by traditional microscopy. observation phase separation giant plasma membrane-derived vesicles from live cells is powerful tool for studying lateral heterogeneity eukaryotic membranes, specifically...

10.1016/j.bpj.2015.03.017 article EN cc-by-nc-nd Biophysical Journal 2015-05-01

Flotillins are prominent, oligomeric protein components of erythrocyte (RBC) membrane raft domains and considered to play an important structural role in lateral organization the plasma membrane. In our previous work on erythroid membranes giant vesicles (GPMVs) derived from them we have shown that formation functional (resting state rafts) depends presence palmitoylated 1 (MPP1/p55), pointing its new physiological role. Exploration molecular mechanism MPP1 function organizing described...

10.1016/j.bbamem.2017.08.021 article EN cc-by-nc-nd Biochimica et Biophysica Acta (BBA) - Biomembranes 2017-09-01

It was suggested that minor differences in the structure of FimH are most likely associated with its adhesion specificities and may determine tropism various Salmonella serovars to different species tissues. We have recently shown adhesins from host-adapted serovars, e.g., Choleraesuis (SCh), bind other glycoprotein receptors compared host-unrestricted Enteritidis (SE). Here we identify porcine calreticulin expressed by swine intestinal cells as a host-specific receptor for SCh adhesin,...

10.3389/fcimb.2017.00326 article EN cc-by Frontiers in Cellular and Infection Microbiology 2017-07-19

MPP1 (membrane palmitoylated protein 1) belongs to the MAGUK (membrane-associated guanylate kinase homologs) scaffolding family. These proteins organize molecules into complexes, thereby maintaining structural heterogeneity of plasma membrane (PM). Our previous results indicated that direct, high-affinity interactions between and flotillins (raft marker proteins) display dominant PM-modulating capacity in erythroid cells. In this study, with high-resolution structured illuminated imaging, we...

10.3390/cells11030311 article EN cc-by Cells 2022-01-18

Signaling complexes are localized to distinct plasma-membrane domains which undergo precise spatiotemporal regulation. A crucial link between membrane dynamics and the small GTPase, H-Ras, has been suggested, connecting localization, clustering scaffolding with its activity signal transduction. Results of this study suggest a relationship MPP1 and/or MPP1-dependent organization H-Ras activation. Namely, we show here that in HEL cells, knock-down lead disruption signaling cascade(s) from...

10.18632/oncotarget.24847 article EN Oncotarget 2018-04-06

Flotillins are the major structural proteins in erythroid raft domains. We have shown previously that dynamic nanoscale organization of domains cells may depend on flotillin-MPP1 interactions. Here, by using molecular simulations and a surface plasmon resonance-based approach we determined high-affinity complexes MPP1 flotillins formed via so far unidentified region within D5 domain MPP1. Significantly, this particular "flotillin binding motif" is key physiological importance, as...

10.1038/s41598-021-93982-3 article EN cc-by Scientific Reports 2021-07-20

Rational drug design and in vitro pharmacology profiling constitute the gold standard development pipelines. Problems arise, however, because this process is often difficult due to limited information regarding complete identification of a molecule's biological activities. The increasing affordability genome-wide next-generation technologies now provides an excellent opportunity understand compound's diverse effects on gene regulation. Here, we used unbiased approach lung colon cancer cell...

10.3390/cancers12040864 article EN Cancers 2020-04-02

Our recent studies have pointed to an important role of the MAGUK family member, MPP1, as a crucial molecule interacting with flotillins and involved in lateral organization erythroid plasma membrane. The palmitoylation MPP1 seems be element this process; however, on direct effect protein–protein or protein–membrane interactions vitro are still challenging due difficulties obtaining functional post-translationally modified recombinant proteins lack comprehensive protocols for purification...

10.3390/membranes11090715 article EN cc-by Membranes 2021-09-17
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