Poster
# 102
Poster |
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6th Internet World Congress for Biomedical Sciences |
Masaharu Terashima(1), Makoto Shimoyama(2), Mikako Tsuchiya(3)
(1)(2)(3)Department of Biochemistry. Shimane Medical University - Izumo. Japan
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Contact address: |
Masaharu Terashima Department of Biochemistry Shimane Medical University Izumo 693-8501 Japan tera@shimane-med.ac.jp |
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[Biochemistry] |
[Cell Biology & Cytology] |
Arginine-specific ADP-ribosylation is a post-translational modification, in which ADP-ribose moiety of NAD is transferred to arginine residues in the target proteins or peptides. Actin, a major constituent in all eukaryotic cells, is one of the most important components of cytoskeletal architecture, and is involved in a numerous cellular processes including phagocytosis, cell locomotion, and maintenance of cell shape. These functions depend on the capacity of actin to polymerize and depolymerize. We previously reported that chicken arginine-specific ADP-ribosyltransferase ADP-ribosylated globular (G-) and filamentous (F-) actins, and that the modification of G-actin inhibited its capacity to polymerize in vitro and in situ, suggesting the involvement of ADP-ribosylation in regulation of the cytoskeletal organization in vivo. In the present study, we demonstrated that ADP-ribosylation of F-actin resulted in the depolymerization of the actin. Thus, ADP-ribosylation may have a role to shift G-F actin equilibrium toward the G-actin through the modification of both G- and F-actins, and participate in the regulation of cytoskeletal reorganization.
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[Biochemistry] |
[Cell Biology & Cytology] |
