Autophagy is a process of self-eating, whereby cytosolic constituents are enclosed by a double-membrane vesicle before delivery to the lysosome for degradation. This is an important process which allows for recycling of nutrients and cellular components and thus plays a critical role in normal cellular homeostasis as well as cell survival during stresses such as starvation or hypoxia. A large number of proteins regulate various stages of autophagy in a complex and still incompletely understood series of events. In this review, we will discuss recent studies which provide a growing body of evidence that actin dynamics and proteins that influence actin nucleation play an important role in the regulation of autophagosome formation and maturation.
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http://dx.doi.org/10.1007/s00018-016-2224-z | DOI Listing |
bioRxiv
December 2024
Department of Biological Sciences, University of Delaware, Newark, DE.
Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament polymerization is critical for enucleation, but the molecular regulatory mechanisms remain poorly understood. We utilized publicly available RNA-seq and proteomics datasets to mine for actin-binding proteins and actin-nucleation factors differentially expressed during human erythroid differentiation and discovered that a focal adhesion protein-Tensin-1-dramatically increases in expression late in differentiation.
View Article and Find Full Text PDFSci Rep
December 2024
Department of Chemical Engineering, Kyoto University, Nishi-kyoku, Kyoto, 615-8510, Japan.
J Biol Chem
December 2024
Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, MN 55455, USA. Electronic address:
Proc Natl Acad Sci U S A
December 2024
Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.
Biomolecules
November 2024
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Competition between bacterial species is a major factor shaping microbial communities. It is possible but remains largely unexplored that competition between bacterial pathogens can be mediated through antagonistic effects of bacterial effector proteins on host systems, particularly the actin cytoskeleton. Using Typhimurium invasion into cells as a model, we demonstrate that invasion is inhibited if the host actin cytoskeleton is disturbed by actin-specific toxins, namely, MARTX actin crosslinking (ACD) and Rho GTPase inactivation (RID) domains, TccC3, and 's own SpvB.
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