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Rho GTPase

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== Function ==
== Function ==
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'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''' and '''RhoC'''. These 3 proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>.
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'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''', '''RhoC''', '''RhoD''' and '''RhoE'''. These 3 proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>. '''Mitochondrial Rho GTPase''' (Miro) have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis<ref>PMID:12482879</ref>.
== Disease ==
== Disease ==
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**[[1gwn]] – mRhoE core domain + GTP <br />
**[[1gwn]] – mRhoE core domain + GTP <br />
**[[2v55]] – hRhoE + ROCKI + GTP + ANP<br />
**[[2v55]] – hRhoE + ROCKI + GTP + ANP<br />
 +
 +
*Miro1
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**[[5kso]], [[5ksp]], [[5ksy]] – hMiro1 C-terminal + GDP <br />
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**[[5ksz]] – hMiro1 EF hand and kinase domain + GMPPCP <br />
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**[[5kty]], [[5ku1]] – hMiro1 EF hand and kinase domain + GDP <br />
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*Miro2
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**[[5kut]] – hMiro2 C-terminal + GDP <br />
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*Miro
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**[[4c0j]], [[4c0k]] – DmMiro – ''Drosophila melanogaster'' <br />
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**[[4c0l]] – DmMiro + GDP <br />
}}
}}
== References ==
== References ==
<references/>
<references/>

Revision as of 10:44, 9 February 2017

Human RhoA (green) complex with RhoGAP (grey), GDP, AlF4 and Mg+2 ion (green) (PDB code 1tx4)

Drag the structure with the mouse to rotate

3D structures of Rho GTPase

Updated on 09-February-2017

References

  1. ↑ Sepp KJ, Auld VJ. RhoA and Rac1 GTPases mediate the dynamic rearrangement of actin in peripheral glia. Development. 2003 May;130(9):1825-35. PMID:12642488
  2. ↑ Fransson A, Ruusala A, Aspenstrom P. Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. J Biol Chem. 2003 Feb 21;278(8):6495-502. Epub 2002 Dec 12. PMID:12482879 doi:http://dx.doi.org/10.1074/jbc.M208609200
  3. ↑ Zhou J, Hayakawa Y, Wang TC, Bass AJ. RhoA mutations identified in diffuse gastric cancer. Cancer Cell. 2014 Jul 14;26(1):9-11. doi: 10.1016/j.ccr.2014.06.022. PMID:25026207 doi:http://dx.doi.org/10.1016/j.ccr.2014.06.022
  4. ↑ Jin L, Burnett AL. RhoA/Rho-kinase in erectile tissue: mechanisms of disease and therapeutic insights. Clin Sci (Lond). 2006 Feb;110(2):153-65. PMID:16411892 doi:http://dx.doi.org/10.1042/CS20050255
  5. ↑ Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ. Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature. 1997 Oct 16;389(6652):758-62. PMID:9338791 doi:10.1038/39651

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