The roles of monomeric GTP-binding proteins in macroautophagy in Saccharomyces cerevisiae.

Int J Mol Sci

Department of Biology, Georgetown University, Washington, DC 20057, USA.

Published: October 2014

Autophagy is a cellular degradation process that sequesters components into a double-membrane structure called the autophagosome, which then fuses with the lysosome or vacuole for hydrolysis and recycling of building blocks. Bulk phase autophagy, also known as macroautophagy, controlled by specific Atg proteins, can be triggered by a variety of stresses, including starvation. Because autophagy relies extensively on membrane traffic to form the membranous structures, factors that control membrane traffic are essential for autophagy. Among these factors, the monomeric GTP-binding proteins that cycle between active and inactive conformations form an important group. In this review, we summarize the functions of the monomeric GTP-binding proteins in autophagy, especially with reference to experiments in Saccharomyces cerevisiae.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4227204PMC
http://dx.doi.org/10.3390/ijms151018084DOI Listing

Publication Analysis

Top Keywords

monomeric gtp-binding
12
gtp-binding proteins
12
saccharomyces cerevisiae
8
membrane traffic
8
autophagy
5
roles monomeric
4
proteins
4
proteins macroautophagy
4
macroautophagy saccharomyces
4
cerevisiae autophagy
4

Similar Publications

Exploiting F NMR in a Multiplexed Assay for Small GTPase Activity.

J Am Chem Soc

January 2025

Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260, United States.

Small GTPases (smG) are a 150-member family of proteins, comprising five subfamilies: Ras, Rho, Arf, Rab, and Ran-GTPases. These proteins function as molecular switches, toggling between two distinct nucleotide-bound states. Using traditional multidimensional heteronuclear NMR, even for single smGs, numerous experiments, high protein concentrations, expensive isotope labeling, and long analysis times are necessary.

View Article and Find Full Text PDF

Polar localization and local translation of RHO-RELATED PROTEIN FROM PLANTS2 mRNAs promote root hair growth in Arabidopsis.

Plant Cell

December 2024

State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, and Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, PR China.

Root hairs are tip-growing cells that anchor plants in the soil and are critical for water uptake, nutrient acquisition, and plant-environment interactions. While the molecular mechanisms that maintain the polar growth of root hairs through the asymmetric distribution of proteins, such as RHO-RELATED PROTEIN FROM PLANTS 2 (ROP2), have been described, it is unclear whether and how the transcripts encoding these tip-localized proteins are polarly localized and locally translated. Here, we demonstrated that ROP2 mRNA exhibits polar localization in Arabidopsis (Arabidopsis thaliana) root hairs.

View Article and Find Full Text PDF

The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear.

View Article and Find Full Text PDF

During growth, cells need to synthesize and expand their envelope, a process that requires careful regulation. Here, we show that the GTPase ObgE of E. coli contributes to the regulation of lipopolysaccharide (LPS) synthesis, an essential component of the Gram-negative outer membrane.

View Article and Find Full Text PDF

mTORC1 restricts TFE3 activity by auto-regulating its presence on lysosomes.

Mol Cell

November 2024

Center for Molecular Medicine, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, the Netherlands; Oncode Institute, Utrecht, the Netherlands. Electronic address:

To stimulate cell growth, the protein kinase complex mTORC1 requires intracellular amino acids for activation. Amino-acid sufficiency is relayed to mTORC1 by Rag GTPases on lysosomes, where growth factor signaling enhances mTORC1 activity via the GTPase Rheb. In the absence of amino acids, GATOR1 inactivates the Rags, resulting in lysosomal detachment and inactivation of mTORC1.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!