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Vimentin Mediates Uptake of C3 Exoenzyme
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Vimentin Mediates Uptake of C3 Exoenzyme
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Journal Article
Vimentin Mediates Uptake of C3 Exoenzyme
2014
Overview
Clostridium botulinum C3 exoenzyme (C3) selectively inactivates RhoA/B/C GTPases by ADP-ribosylation. Based on this substrate specificity C3 is a well-established tool in cell biology. C3 is taken up by eukaryotic cells although lacking an uptake and translocation domain. Based on different approaches vimentin was identified as membranous C3-interaction partner by mass spectrometry. Vimentin in fact was partly localized at the outer surface of hippocampal HT22 cells and J744A.1 macrophages. Domain analysis identified the rod domain as binding partner of C3. Vimentin was also involved in uptake of C3 as shown by knock down of vimentin in HT22 and J774A.1 cells. The involvement of vimentin in uptake of C3 was further supported by the findings that the vimentin disruptor acrylamide blocked uptake of C3. Vimentin is not only a major organizing element of the intermediate filament network but is also involved in both binding and uptake of C3 exoenzyme.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ ADP Ribose Transferases - genetics
/ ADP Ribose Transferases - isolation & purification
/ ADP Ribose Transferases - metabolism
/ Animals
/ Binding
/ Botulinum Toxins - isolation & purification
/ Botulinum Toxins - metabolism
/ Carrier Proteins - metabolism
/ Cholera
/ Intermediate filament proteins
/ Mice
/ Neurons
/ Protein Interaction Domains and Motifs
/ RNA, Small Interfering - genetics
/ Vimentin
