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Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors

Olson, Michael F.·2018·Small GTPases
DOI 10.1080/21541248.2016.1218407PMC PMC5927519
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Figure 1. Filamentous actin structures. MDA MB 231 human breast cancer cells were fixed and stained with fluorescently labeled phalloidin to visualize filamentous actin structures. The image shows a maximum-projection assembled from 22 Z-plane images acquired with a Zeiss LSM 880 Airyscan microscope.
Figure 1. Filamentous actin structures. MDA MB 231 human breast cancer cells were fixed and stained with fluorescently labeled phalloidin to visualize filamentous actin structures. The image shows a maximum-projection assembled from 22 Z-plane images acquired with a Zeiss LSM 880 Airyscan microscope.CC BY-NC · PubMed Central
Figure 2. Rho GTPases are molecular switches. When associated GEF molecules promote GDP release, GTP is bound which results in conformational changes in the Switch 1 and Switch 2 regions that enable interactions with downstream effector proteins and consequent signal transduction. Upon association with GAPs, GTP is hydrolysed to GDP and Pi is released to inactivate the Rho protein.
Figure 2. Rho GTPases are molecular switches. When associated GEF molecules promote GDP release, GTP is bound which results in conformational changes in the Switch 1 and Switch 2 regions that enable interactions with downstream effector proteins and consequent signal transduction. Upon association with GAPs, GTP is hydrolysed to GDP and Pi is released to inactivate the Rho protein.CC BY-NC · PubMed Central
Figure 3. The Rho GTPase family. (A) An amino acid identity matrix was generated by comparing the primary sequence of 20 human Rho proteins. Grouping into Rac (red), Rho (purple), RhoH (brown) and RhoBTB (green) groups was by hierarchical clustering using the Multalin multiple sequence alignment program.16 (B) A rooted phylogenetic tree of the 20 human Rho GTPases was generated by hierarchical clusing using the Multalin multiple sequence alignment program.16 Distances between proteins are proportional to their PAM (point accepted mutation) score of molecular evolution.
Figure 3. The Rho GTPase family. (A) An amino acid identity matrix was generated by comparing the primary sequence of 20 human Rho proteins. Grouping into Rac (red), Rho (purple), RhoH (brown) and RhoBTB (green) groups was by hierarchical clustering using the Multalin multiple sequence alignment program.16 (B) A rooted phylogenetic tree of the 20 human Rho GTPases was generated by hierarchical clusing using the Multalin multiple sequence alignment program.16 Distances between proteins are proportional to their PAM (point accepted mutation) score of molecular evolution.CC BY-NC · PubMed Central
Figure 4. Amino acid conservation in the Rho GTPases. (A) The core conserved segments, with important features numbered by their positions within amino acids 4–177 of Rac1, of the 18 most related Rho GTPases are depicted with percentages of amino acid identity ranging from 100% (red) to less than 50% (white). Guanine nucleotide binding regions are shown as G1 to G5 boxes (green). Switch 1 (yellow) and Switch 2 (magenta) regions are also depicted. (B) Rac2-GDP (PDB ID: 2W2T) structure was rendered with Chimera,112 with G boxes (green), Switch 1 (yellow) and Switch 2 (magenta) regions indicated. (C) Amino acid identity for 18 Rho GTPases was determined with Clustal Omega 113 and mapped onto Rac2-GDP with Chimera. Colors depicting amino acid identity from 100% (red) to 0% (blue) as indicated.
Figure 4. Amino acid conservation in the Rho GTPases. (A) The core conserved segments, with important features numbered by their positions within amino acids 4–177 of Rac1, of the 18 most related Rho GTPases are depicted with percentages of amino acid identity ranging from 100% (red) to less than 50% (white). Guanine nucleotide binding regions are shown as G1 to G5 boxes (green). Switch 1 (yellow) and Switch 2 (magenta) regions are also depicted. (B) Rac2-GDP (PDB ID: 2W2T) structure was rendered with Chimera,112 with G boxes (green), Switch 1 (yellow) and Switch 2 (magenta) regions indicated. (C) Amino acid identity for 18 Rho GTPases was determined with Clustal Omega 113 and mapped onto Rac2-GDP with Chimera. Colors depicting amino acid identity from 100% (red) to 0% (blue) as indicated.CC BY-NC · PubMed Central
Figure 5. Phosphorylation and ubiquitylation of Rho GTPases. (A) Phosphorylation (purple) and ubiquitylation (brown) events reported in the literature or PhosphoSite (www.phosphosite.org) were mapped onto the amino acid identity grid depicting the core conserved segments, analogous to amino acids 4–177 of Rac1, of the 18 most related Rho GTPases, ranging from 100% identity (salmon) to less than 50% (white). (B) The phosphorylations (purple) and ubiquitylations (brown) of Rac2 were mapped onto the 3-dimensional structure, with G boxes (green), Switch 1 (yellow) and Switch 2 (magenta) regions depicted. (C) View rotated 180° of Rac2 phosphorylations and ubiquitylations.
Figure 5. Phosphorylation and ubiquitylation of Rho GTPases. (A) Phosphorylation (purple) and ubiquitylation (brown) events reported in the literature or PhosphoSite (www.phosphosite.org) were mapped onto the amino acid identity grid depicting the core conserved segments, analogous to amino acids 4–177 of Rac1, of the 18 most related Rho GTPases, ranging from 100% identity (salmon) to less than 50% (white). (B) The phosphorylations (purple) and ubiquitylations (brown) of Rac2 were mapped onto the 3-dimensional structure, with G boxes (green), Switch 1 (yellow) and Switch 2 (magenta) regions depicted. (C) View rotated 180° of Rac2 phosphorylations and ubiquitylations.CC BY-NC · PubMed Central

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Metadata

Authors
Olson, M. F.
Affiliations
Cancer Research UK Beatson Institute, Garscube Estate, Glasgow, UK
Venue
Small GTPases
Publisher
Informa UK Limited
Published
2016-08-22
Volume
9
Issue
3
Pages
203-215
ISSN
  • 2154-1248
  • 2154-1256
DOI
10.1080/21541248.2016.1218407
PMC
PMC5927519
Cited by
96
References
10
Language
en
Licence
creativecommons.org/licenses/by-nc/3.0/ (vor)
Funders
  • Cancer Research UK (A18276)
  • Medical Research Council (MR/M018776/1)
  • Engineering and Physical Sciences Research Council (EP/N014642/1)

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Olson, M. F. (2018). Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors. Small GTPases. https://doi.org/10.1080/21541248.2016.1218407