A5022636758- Fibroblast Growth Factor Research
- Erythrocyte Function and Pathophysiology
- Cellular transport and secretion
- Lipid Membrane Structure and Behavior
- Proteoglycans and glycosaminoglycans research
- Advanced Fluorescence Microscopy Techniques
- Pancreatic function and diabetes
- Endoplasmic Reticulum Stress and Disease
- Cancer, Hypoxia, and Metabolism
- Phagocytosis and Immune Regulation
- Retinal Development and Disorders
- Connective tissue disorders research
- Skin and Cellular Biology Research
- Photochromic and Fluorescence Chemistry
- bioluminescence and chemiluminescence research
- Neonatal Respiratory Health Research
- Angiogenesis and VEGF in Cancer
- RNA Interference and Gene Delivery
Heidelberg University
2019-2024
Heidelberg University
2019-2024
Helsinki Institute of Physics
2023
University of Helsinki
2023
University Hospital Heidelberg
2023
Czech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry
2023
Freie Universität Berlin
2023
Abstract We developed a system for optogenetic release of single molecules in cells. confined soluble and transmembrane proteins to the Golgi apparatus via photocleavable protein released them by short pulses light. Our method allows light dose-dependent delivery functional cytosol plasma membrane amounts compatible with single-molecule imaging, greatly simplifying access microscopy any live were able reconstitute ion conductance delivering BK LRRC8/volume-regulated anion channels membrane....
Fibroblast growth factor 2 (FGF2) is a tumor cell survival that transported into the extracellular space by an unconventional secretory mechanism. Cell surface heparan sulfate proteoglycans are known to play essential role in this process. Unexpectedly, we found among diverse subclasses consisting of syndecans, perlecans, glypicans, and others, Glypican-1 (GPC1) principle rate-limiting drives secretion FGF2. By contrast, demonstrate GPC1 be dispensable for FGF2 signaling cells. We provide...
Abstract FGF2 is a tumor cell survival factor that exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein secretion based on direct translocation across the plasma membrane. The Na,K-ATPase has previously been shown to play role in this process, however, underlying remained elusive. Here, we define structural elements are critical for physical interaction between and α1 subunit Na,K-ATPase. In intact cells, corresponding mutant forms were...
FGF2 is a cell survival factor involved in tumor-induced angiogenesis that secreted through an unconventional secretory pathway based upon direct protein translocation across the plasma membrane. Here, we demonstrate both PI(4,5)P2-dependent recruitment at inner membrane leaflet and into extracellular space are positively modulated by cholesterol living cells. We further revealed to enhance binding PI(4,5)P2-containing lipid bilayers. Based on extensive atomistic molecular dynamics (MD)...
Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated phosphatidylinositol-4,5-bisphosphate (PI(4,5)P )-dependent formation highly dynamic FGF2 oligomers at inner membrane leaflet, inducing lipidic pores. Cell surface heparan sulfate chains linked to glypican-1 (GPC1) capture outer completing into extracellular space. While basic steps this are well understood,...
Summary Fibroblast Growth Factor 2 (FGF2) is a cell survival factor involved in tumor-induced angiogenesis. FGF2 secreted through an unconventional secretory pathway based upon direct protein translocation across the plasma membrane. Here we demonstrate that both PI(4,5)P -dependent recruitment at inner membrane leaflet and into extracellular space are positively modulated by cholesterol living cells. We further reveal to enhance binding -containing lipid bilayers fully reconstituted system....
Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated phosphatidylinositol-4,5-bisphosphate (PI(4,5)P )-dependent formation highly dynamic FGF2 oligomers at inner membrane leaflet, inducing lipidic pores. Cell surface heparan sulfate chains linked to glypican-1 (GPC1) capture outer completing into extracellular space. While basic steps this are well understood,...
Fibroblast Growth Factor 2 (FGF2) is a potent mitogen secreted from mammalian cells through an unconventional secretory pathway. This process mediated by direct translocation of FGF2 across the plasma membrane into extracellular space. It requires several components that are asymmetrically distributed between two leaflets membrane. At inner leaflet, undergoes sequential interactions with Na,K-ATPase, Tec kinase, and phosphoinositide PI(4,5)P2. While kinase auxiliary factors, PI(4,5)P2...
Fibroblast Growth Factor 2 (FGF2) is a potent mitogen secreted from mammalian cells through an unconventional secretory pathway. This process mediated by direct translocation of FGF2 across the plasma...
Fibroblast Growth Factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated PI(4,5)P -dependent formation highly dynamic FGF2 oligomers at inner membrane leaflet, inducing lipidic pores. Cell surface heparan sulfate chains linked to glypican-1 (GPC1) capture outer completing into extracellular space. While basic steps this are well understood, molecular mechanism which oligomerizes on...
Fibroblast Growth Factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated PI(4,5)P -dependent formation highly dynamic FGF2 oligomers at inner membrane leaflet, inducing lipidic pores. Cell surface heparan sulfate chains linked to glypican-1 (GPC1) capture outer completing into extracellular space. While basic steps this are well understood, molecular mechanism which oligomerizes on...
Abstract Fibroblast Growth Factor 2 (FGF2) is a tumor cell survival factor that transported into the extracellular space by an unconventional secretory mechanism. Cell surface heparan sulfate proteoglycans are known to play essential role in this process. Unexpectedly, we found among diverse sub-classes consisting of syndecans, perlecans, glypicans and others, Glypican-1 (GPC1) both principle rate-limiting drives secretion FGF2. By contrast, demonstrate GPC1 be dispensable for FGF2 signaling...
Summary Fibroblast Growth Factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated PI(4,5)P -dependent formation highly dynamic FGF2 oligomers at inner membrane leaflet, inducing lipidic pores. Cell surface heparan sulfate chains linked to glypican-1 (GPC1) capture outer completing into extracellular space. While basic steps this are well understood, molecular mechanism which oligomerizes...
We developed a system for optogenetic release of single molecules in live cells. confined soluble and transmembrane proteins to the Golgi apparatus via photocleavable protein released them by short pulses light. Our method allows controlled delivery functional cytosol plasma membrane amounts compatible with molecule imaging, greatly simplifying access microscopy any Furthermore, we could reconstitute cellular functions such as ion conductance delivering BK VRAC channels membrane. Finally,...
Summary Fibroblast Growth Factor 2 (FGF2) is a tumor cell survival factor that exported from cells by an unconventional secretory pathway. This process based on direct translocation of FGF2 across the plasma membrane. membrane depends PI(4,5)P -induced formation membrane-inserted oligomers followed extracellular trapping at outer leaflet mediated surface heparan sulfate proteoglycans. Beyond well-characterized core mechanism translocation, Na,K-ATPase has been proposed to play so far unknown...