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Structure of an LGR dimer - an evolutionary predecessor of glycoprotein hormone receptors.
bioRxiv
January 2025
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
The glycoprotein hormones of humans, produced in the pituitary and acting through receptors in the gonads to support reproduction and in the thyroid gland for metabolism, have co-evolved from invertebrate counterparts. These hormones are heterodimeric cystine-knot proteins; and their receptors bind the cognate hormone at an extracellular domain and transmit the signal of this binding through a transmembrane domain that interacts with a heterotrimeric G protein. Structures determined for the human receptors as isolated for cryogenic electron microscopy (cryo-EM) are all monomeric despite compelling evidence for their functioning as dimers.
View Article and Find Full Text PDFHomeodomain Involvement in Nuclear HOX Protein Homo- and Heterodimerization.
Int J Mol Sci
January 2025
Louvain Institute of Molecular Science and Technology, Université catholique de Louvain, 5 (L7.07.10) Place Croix du Sud, 1348 Louvain-la-Neuve, Belgium.
genes play essential roles in patterning the anteroposterior axis of animal embryos and in the formation of various organs. In mammals, there are 39 genes organized into four clusters (HOXA-D) located on different chromosomes. In relationship with their orderly arrangement along the chromosomes, these genes show nested expression patterns which imply that embryonic territories co-express multiple genes along the main body axis.
View Article and Find Full Text PDFPhysiological, Photosynthetic Characteristic and Transcriptome Analysis of Transgenic × Under Salt Stress.
Int J Mol Sci
December 2024
College of Forestry, Henan Agricultural University, Zhengzhou 450002, China.
The WRKY70 transcription factor (TF) was reported to play an important role in the salt stress response mechanism of in our previous research, and we also produced several overexpression (OEXs) and RNAi suppression (REXs) × lines. In order to further compare the photosynthetic and physiological characteristics of NT (non-transgenic line) and transgenic lines under salt stress, the dynamic phenotypic change, Na and K content in leaf and root tissues, superoxide dismutase (SOD) and peroxidase (POD) activity, malondialdehyde (MDA) content, chlorophyll content (Chl), photosynthesis parameters (net photosynthetic rate, P; stomatal conductance, Gs; intercellular CO concentration, C; transpiration rate, T), chlorophyll fluorescence parameters (electron transport rate, ETR; maximum photochemical efficiency of photosystem II (PSII), F/F; actual efficiency of PSII, Φ; photochemical quenching coefficient, q; non-photochemical quenching, NPQ; the photosynthetic light-response curves of Φ and ETR) and RNA-seq of NT, OEX and REX lines were detected and analyzed. The phenotypic observation, MDA content and Chl detection results indicate that the stress damage of REXs was less severe than that of NT and OEX lines under salt stress.
View Article and Find Full Text PDFThe α- and β-Subunits of Nitric Oxide-Sensitive Guanylyl Cyclase in Pericytes of Healthy Human Dental Pulp.
Int J Mol Sci
December 2024
Institute of Physiology, University of Würzburg, 97070 Würzburg, Germany.
Nitric oxide-sensitive guanylyl cyclase (NO-GC) is a heterodimeric enzyme with an α- and a β-subunit. In its active form as an αβ-heterodimer, NO-GC produces cyclic guanosine-3',5'-monophophate (cGMP) to regulate vasodilation and proliferation of vascular smooth muscle cells (VSMCs). In contrast to VSMCs, only a few studies reported on the expression of the NO-GC αβ-heterodimer in human pericytes.
View Article and Find Full Text PDFSurprising features of nuclear receptor interaction networks revealed by live-cell single-molecule imaging.
Elife
January 2025
Department of Molecular and Cell Biology, Berkeley, United States.
Type II nuclear receptors (T2NRs) require heterodimerization with a common partner, the retinoid X receptor (RXR), to bind cognate DNA recognition sites in chromatin. Based on previous biochemical and overexpression studies, binding of T2NRs to chromatin is proposed to be regulated by competition for a limiting pool of the core RXR subunit. However, this mechanism has not yet been tested for endogenous proteins in live cells.
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