The intracellular migration of G protein in vesicular stomatitis virus-infected cells was visualized by light and electron microscope radioautography after a 2-min pulse with [3H]mannose followed by nonradioactive chase for various intervals. The radioactivity initially (at 5-10 min) appeared predominantly in the endoplasmic reticulum, and the [3H]mannose-labeled G protein produced was sensitive to endoglycosidase H. Silver grains were subsequently (at 30-40 min) observed over the Golgi apparatus, and the [3H]mannose-labeled G protein became resistant to endoglycosidase H digestion. Our data directly demonstrate the intracellular transport of a plasmalemma-destined transmembrane glycoprotein through the Golgi apparatus.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112182 | PMC |
http://dx.doi.org/10.1083/jcb.94.1.36 | DOI Listing |
Planta
January 2025
Institute of Plant Biology, National Taiwan University, Taipei, Taiwan.
PME12-mutated plants displayed altered stomatal characteristics and susceptibility to ABA-induced closure. Despite changes in PME activity, the mutant exhibited enhanced thermotolerance. These findings suggest a complex interplay between pectin methylesterification, ABA response, and stomatal function, contributing to plant adaptation to heat stress.
View Article and Find Full Text PDFBackground: G protein-coupled receptors (GPCRs) are associated with multiple stages of the pathophysiology of Alzheimer's disease (AD). Biased GPCR signaling preferentially activates G protein- or β-arrestin-mediated signaling pathways and presents opportunities to develop more selective and safer therapeutics but remains largely unexplored in AD. Recently, we developed a G protein-biased GPR3 AD mouse model, which does not recruit β-arrestin 2, that displays reduced amyloid-β (Aβ) pathology without adverse cognitive effects associated with elimination of both G protein and β-arrestin signaling.
View Article and Find Full Text PDFCell Mol Life Sci
January 2025
Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Glycans are known to be fundamental for many cellular and physiological functions. Congenital disorders of glycosylation (CDG) currently encompassing over 160 subtypes, are characterized by glycan synthesis and/or processing defects. Despite the increasing number of CDG patients, therapeutic options remain very limited as our knowledge on glycan synthesis is fragmented.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Murdoch Children's Research Institute, Melbourne, VIC 3052, Australia.
The TRAPP (TRAnsport Protein Particle) protein complex is a multi-subunit complex involved in vesicular transport between intracellular compartments. The TRAPP complex plays an important role in endoplasmic reticulum-to-Golgi and Golgi-to-plasma membrane transport, as well as autophagy. TRAPP complexes comprise a core complex, TRAPPI, and the association of peripheral protein subunits to make two complexes, known as TRAPPII and TRAPPIII, which act as Guanine Nucleotide Exchange Factors (GEFs) of Rab11 and Rab1, respectively.
View Article and Find Full Text PDFBiomolecules
November 2024
School of Medicine, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China.
Autophagy is an important catabolic process to maintain cellular homeostasis and antagonize cellular stresses. The initiation and activation are two of the most important aspects of the autophagic process. This review focuses on mechanisms underlying autophagy initiation and activation and signaling pathways regulating the activation of autophagy found in recent years.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!