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. 2020 May 2;9(5):1328. doi: 10.3390/jcm9051328

Figure 1.

Figure 1

(A) Structure of Rho-associated coiled-coil containing kinase (ROCK) 1 and ROCK2. Both isoforms consist of a N-terminal kinase domain, a coiled-coil domain containing a Rho binding domain (RBD), a pleckstrin homology (PH) motif and a C-terminal cysteine-rich domain. ROCK1 and ROCK2 share 65% overall homology in amino acid sequence. (B) Inactivation/activation of ROCK. When the N-terminus is next to C-terminus, i.e., showing a closed configuration, the ROCK is inactive because of the auto-inhibitory loop. The opening of the loop can be caused 1) by caspase-3, or caspase-2 and granzyme B, that cleave the C-terminus of ROCK1 and ROCK2, respectively, or 2) by a Rho-dependent pathway, via binding of GTP-RhoA to the RBD, driven by angiotensin II, endothelin (ET) 1, fibroblast growth factor (FGF) and TGFβ, interleukin (IL)-1 or interferon γ. Modified from Hartmann, S., et al. [2] and Shimizu, T., et al. [3].