[HTML][HTML] Vimentin mediates uptake of C3 exoenzyme

A Rohrbeck, A Schröder, S Hagemann, A Pich… - PLoS …, 2014 - journals.plos.org
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 …

[HTML][HTML] Uptake of Clostridium botulinum C3 exoenzyme into intact HT22 and J774A. 1 cells

A Rohrbeck, L Von Elsner, S Hagemann, I Just - Toxins, 2015 - mdpi.com
The Clostridium botulinum C3 exoenzyme selectively ADP-ribosylates low molecular weight
GTP-binding proteins RhoA, B and C. This covalent modification inhibits Rho signaling …

Cell Entry of C3 Exoenzyme from Clostridium botulinum

A Rohrbeck, I Just - Uptake and Trafficking of Protein Toxins, 2017 - Springer
Clostridium botulinum C3 is the prototype of C3-like ADP-ribosyltransferases that selectively
ADP-ribosylate the small GTP-binding proteins RhoA/B/C and inhibit their downstream …

Binding of Clostridium botulinum C3 exoenzyme to intact cells

A Rohrbeck, L von Elsner, S Hagemann… - … Schmiedeberg's archives of …, 2014 - Springer
C3 from Clostridium botulinum (C3) specifically modifies Rho GTPases RhoA, RhoB, and
RhoC by mono-ADP-ribosylation. The confined substrate profile of C3 is the basis for its use …

The intermediate filament protein vimentin is essential for axonotrophic effects of Clostridium botulinum C3 exoenzyme

A Adolf, G Leondaritis, A Rohrbeck… - Journal of …, 2016 - Wiley Online Library
The type III intermediate filament protein vimentin was recently identified to mediate binding
and uptake of Clostridium botulinum C3 exoenzyme (C3bot) in two cell lines. Here, we used …

Clostridium botulinum C3 exoenzyme: Rho-inactivating tool in cell biology and a neurotrophic agent

I Just, SC Huelsenbeck, H Genth - The Open Toxinology …, 2010 - benthamopen.com
C3 exoenzyme from Clostridium botulinum is the prototype of bacterial ADP-
ribosyltransferases, which selectively modifies the Rho isoforms RhoA, RhoB and RhoC by …

Inhibition of macrophage migration by C. botulinum exoenzyme C3

J Rotsch, A Rohrbeck, M May, T Kolbe… - Naunyn-Schmiedeberg's …, 2012 - Springer
C3-like exoenzymes are produced by various microorganism including Clostridium
botulinum (C3bot), Bacillus cereus and Staphylococcus aureus. C3bot is the prototype of C3 …

Selective and specific internalization of clostridial C3 ADP‐ribosyltransferases into macrophages and monocytes

J Fahrer, J Kuban, K Heine, G Rupps… - Cellular …, 2010 - Wiley Online Library
The C3 transferases from Clostridium botulinum (C3bot) and Clostridium limosum (C3lim)
mono‐ADP‐ribosylate and thereby inactivate RhoA,‐B and‐C of eukaryotic cells. Due to …

[HTML][HTML] The Rho ADP-ribosylating C3 exoenzyme binds cells via an Arg–Gly–Asp motif

A Rohrbeck, M Höltje, A Adolf, E Oms… - Journal of Biological …, 2017 - ASBMB
The Rho ADP-ribosylating C3 exoenzyme (C3bot) is a bacterial protein toxin devoid of a cell-
binding or-translocation domain. Nevertheless, C3 can efficiently enter intact cells, including …

Release of astroglial vimentin by extracellular vesicles: Modulation of binding and internalization of C3 transferase in astrocytes and neurons

A Adolf, A Rohrbeck, A Münster‐Wandowski… - Glia, 2019 - Wiley Online Library
Clostridium botulinum C3 transferase (C3bot) ADP‐ribosylates rho proteins to change
cellular functions in a variety of cell types including astrocytes and neurons. The …