Publications

In bacteria, the GntR family is a widespread family of transcription factors responsible for the regulation of a myriad of biological processes. In contrast, despite their occurrence in archaea only a little information is available on the function of GntR-like transcription factors in this domain of life. The thermoacidophilic crenarchaeon Sulfolobus acidocaldarius harbors a GntR-like regulator belonging to the YtrA subfamily, encoded as the ...

Cell polarity reflected by asymmetric distribution of proteins at the plasma membrane is a fundamental feature of unicellular and multicellular organisms. It remains conceptually unclear how cell polarity is kept in cell wall-encapsulated plant cells. We have used super-resolution and semi-quantitative live-cell imaging in combination with pharmacological, genetic, and computational approaches to reveal insights into the mechanism of cell ...

BACKGROUND: Membrane proteins (MPs) are an important class of molecules with a wide array of cellular functions and are part of many metabolic pathways. Despite their great potential-as therapeutic drug targets or in microbial cell factory optimization-many challenges remain for efficient and functional expression in a host such as Escherichia coli. RESULTS: A dynamically regulated small RNA-based circuit was developed to counter membrane stress ...

The transmembrane domain recognition complex (TRC) pathway is required for the insertion of C-terminal tail-anchored (TA) proteins into the lipid bilayer of specific intracellular organelles such as the endoplasmic reticulum (ER) membrane. In order to facilitate correct insertion, the recognition complex (consisting of BAG6, GET4 and UBL4A) must first bind to TA proteins and then to GET3 (TRC40, ASNA1), which chaperones the protein to the ER ...

PDZ (PSD-95/Discs-large/ZO-1) domains are key components of scaffold proteins acting as hubs controlling the specificity, dynamics and flow of cellular information. The original view envisioned PDZ domains as protein-protein interactions domains supporting the assembly of multiprotein complexes at the membrane. Their ability to organize signaling complexes was mainly attributed to their ability to bind the C-terminal ends of a plethora of ...

Upon encountering the sudden, lethal activity of antibiotics, survival of a bacterial population largely depends on the presence of a small fraction of transiently stressresistant cells that protect the population from eradication. These so-called persisters are genetically identical to other cells in the population and are therefore phenotypic variants. As a bet-hedging strategy, persistence levels are determined both by stochastic induction ...

Membrane proteins are an important class of molecules with a wide array of cellular functions and are part of many metabolic pathways. Despite their great potential to be used as therapeutic drug targets or in microbial cell factory optimisation, many challenges remain for efficient and functional expression in a host such as Escherichia coli. Recent progress in metabolic engineering and synthetic biology could disclose membrane proteins for ...

Presenilins (PSs) are components of the gamma-secretase complex that mediates intramembranous cleavage of type I membrane proteins. We show that gamma-secretase is involved in the regulation of cellular lipoprotein uptake. Loss of gamma-secretase function decreased endocytosis of low-density lipoprotein (LDL) receptor. The decreased uptake of lipoproteins led to upregulation of cellular cholesterol biosynthesis by increased expression of CYP51 ...

The polarized architecture of epithelia relies on an interplay between the cytoskeleton, the trafficking machinery, and cell-cell and cell-matrix adhesion. Specifically, contact with the basement membrane (BM), an extracellular matrix underlying the basal side of epithelia, is important for cell polarity. However, little is known about how BM proteins themselves achieve a polarized distribution. In a genetic screen in the Drosophila follicular ...

In plants, clathrin-mediated endocytosis (CME) is dependent on the function of clathrin and its accessory heterooligomeric adaptor protein complexes, ADAPTOR PROTEIN2 (AP-2) and the TPLATE complex (TPC), and is negatively regulated by the hormones auxin and salicylic acid (SA). The details for how clathrin and its adaptor complexes are recruited to the plasma membrane (PM) to regulate CME, however, are poorly understood. We found that SA and the ...