Hsc70 is a Component of Bacterially Generated Actin-Rich Structures: An Immunolocalization Study.
Brittany D WalkerMichael D ChuaJulian A GuttmanPublished in: Anatomical record (Hoboken, N.J. : 2007) (2018)
Enteropathogenic Escherichia coli (EPEC), Salmonella typhimurium, and Listeria monocytogenes usurp the actin cytoskeleton for their attachment, internalization and transport within and amongst infected cells. To try to gain a greater understanding of the molecular components utilized by these microbes during their infections we previously concentrated actin-rich structures generated during EPEC infections (called pedestals) and identified the heat shock cognate 70 protein (Hsc70) as a potential candidate. This multifunctional protein classically acts as a chaperone for the proper folding of a variety of proteins and is involved in uncoating clathrin from coated pits. Here we demonstrated that Hsc70 is recruited to actin structures generated during EPEC, Listeria and Salmonella infections, but not to the same location as clathrin. Anat Rec, 301:2095-2102, 2018. © 2018 Wiley Periodicals, Inc.
Keyphrases
- listeria monocytogenes
- heat shock
- escherichia coli
- cell migration
- heat shock protein
- high resolution
- heat stress
- induced apoptosis
- protein protein
- oxidative stress
- cell cycle arrest
- amino acid
- binding protein
- molecular dynamics simulations
- risk assessment
- cell death
- mass spectrometry
- signaling pathway
- small molecule
- pseudomonas aeruginosa
- type iii