Nucleotide binding switches the information flow in ras GTPases.
The Ras superfamily comprises many guanine nucleotide-binding proteins (G proteins) that are essential to intracellular signal transduction. The guanine nucleotide-dependent intrinsic flexibility patterns of five G proteins were investigated in atomic ...
Francesco Raimondi+3 more
doaj +1 more source
The Targeting of the atToc159 Preprotein Receptor to the Chloroplast Outer Membrane is Mediated by its GTPase Domain and is Regulated by GTP [PDF]
The multimeric translocon at the outer envelope membrane of chloroplasts (Toc) initiates the recognition and import of nuclear-encoded preproteins into chloroplasts.
Hiltbrunner, Andreas+3 more
core +2 more sources
Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts
GGDEF-containing proteins respond to different environmental cues to finely modulate cyclic diguanylate (c-di-GMP) levels in time and space, making the allosteric control a distinctive trait of the corresponding proteins.
Federico Mantoni+10 more
doaj +1 more source
The chloroplast import receptor Toc34 functions as preprotein-regulated GTPase [PDF]
Toc34 is a protein of the chloroplast outer envelope membrane that acts as receptor for preproteins containing a transit sequence. The recognition of preproteins by Toc34 is regulated by GTP binding and phosphorylation.
Hörth, P.+5 more
core +1 more source
This Is the End: Regulation of Rab7 Nucleotide Binding in Endolysosomal Trafficking and Autophagy
Rab7 – or in yeast, Ypt7p – governs membrane trafficking in the late endocytic and autophagic pathways. Rab7 also regulates mitochondrion-lysosome contacts, the sites of mitochondrial fission.
Christopher Stroupe
doaj +1 more source
Structural Insights into How Yrb2p Accelerates the Assembly of the Xpo1p Nuclear Export Complex
Proteins and ribonucleoproteins containing a nuclear export signal (NES) assemble with the exportin Xpo1p (yeast CRM1) and Gsp1p-GTP (yeast Ran-GTP) in the nucleus and exit through the nuclear pore complex.
Masako Koyama+2 more
doaj +1 more source
Structure and function of bacterial dynamin-like proteins [PDF]
Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core +1 more source
Molecular mechanism of Gαi activation by non-GPCR proteins with a Gα-Binding and Activating motif [PDF]
Heterotrimeric G proteins are quintessential signalling switches activated by nucleotide exchange on Gα. Although activation is predominantly carried out by G-protein-coupled receptors (GPCRs), non-receptor guanine-nucleotide exchange factors (GEFs) have
Baillie, George S.+14 more
core +1 more source
In silico docking of forchlorfenuron (FCF) to septins suggests that FCF interferes with GTP binding.
Septins are GTP-binding proteins that form cytoskeleton-like filaments, which are essential for many functions in eukaryotic organisms. Small molecule compounds that disrupt septin filament assembly are valuable tools for dissecting septin functions with
Dimitrios Angelis+3 more
doaj +1 more source
GTP-Binding Proteins and Regulated Exocytosis [PDF]
Regulated exocytosis, which occurs in response to stimuli, is a two-step process involving the docking of secretory granules (SGs) at specific sites on the plasma membrane (PM), with subsequent fusion and release of granule contents. This process plays a crucial role in a number of tissues, including exocrine glands, chromaffin cells, platelets, and ...
openaire +3 more sources