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Hsc70 is a Component of Bacterially Generated Actin‐Rich Structures: An Immunolocalization Study
Author(s) -
Walker Brittany D.,
Chua Michael D.,
Guttman Julian A.
Publication year - 2018
Publication title -
the anatomical record
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.678
H-Index - 62
eISSN - 1932-8494
pISSN - 1932-8486
DOI - 10.1002/ar.23955
Subject(s) - actin , microbiology and biotechnology , listeria monocytogenes , salmonella , biology , internalization , clathrin , actin cytoskeleton , heat shock protein , chaperone (clinical) , cytoskeleton , endocytosis , bacteria , biochemistry , cell , genetics , gene , medicine , pathology
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.