Rac: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
Michal Harel (talk | contribs)
31,761 edits
No edit summary
 
(11 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<StructureSection load='2h7v' size='450' side='right' caption='Human Rac1 (magenta) complex with YpkA (cyan), GDP and Mg+2 ion (green) (PDB code [[2h7v]])' scene='75/752232/Cv/1' pspeed='8'>
<StructureSection load='' size='350' side='right' caption='Human Rac1 (magenta) complex with YpkA (cyan), GDP and Mg+2 ion (green) (PDB code [[2h7v]])' scene='75/752232/Cv/1' pspeed='8'>


== Function ==
== Function ==
The small G-protein '''Rac''' or '''Ras-related C3 botulinum toxin substrate'''.  '''Ras1''' is involved in the regulation of cytoskeletal organization, cell adhesion, migration and morphological changes<ref>PMID:23412604</ref>.  '''Ras3''' binds to a variety of effector proteins to regulate cellular responses like cell spreading and the formation of actin-based protrusions.
The small G-protein '''Rac''' or '''Ras-related C3 botulinum toxin substrate'''.   
*'''Rac1''' is involved in the regulation of cytoskeletal organization, cell adhesion, migration and morphological changes<ref>PMID:23412604</ref>.   
*'''Rac2''' is expressed in hematopoietic cells exclusively<ref>PMID:32542921</ref>.
* '''Rac3''' binds to a variety of effector proteins to regulate cellular responses like cell spreading and the formation of actin-based protrusions.


== Disease ==  
== Disease ==  
Line 8: Line 11:


== Structural highlights ==
== Structural highlights ==
The interactions between Rac1 and YpkA are via <scene name='75/752232/Cv/7'>switch I and switch II of Rac1 and a helical portion of the protein kinase YpkA</scene><ref>PMID:16959567</ref>. <scene name='75/752232/Cv/6'>GDP binding site on Rac1</scene>.
The interactions between Rac1 and YpkA are via <scene name='75/752232/Cv/8'>switch I and switch II of Rac1 and a helical portion of the protein kinase YpkA</scene><ref>PMID:16959567</ref>. <scene name='75/752232/Cv/9'>GDP binding site on Rac1</scene>.


</StructureSection>
==3D structures of Rac==
==3D structures of Rac==
[[Rac 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Rac1
 
**[[3th5]], [[1ryh]], [[1mh1]] – hRac1 + GNP – human<br />
**[[2p2l]], [[1ryf]] – hRac1 + GDP <br />
**[[4gzl]], [[3sbd]], [[3sbe]] – hRac1 (mutant) + GNP <br />
**[[4gzm]] – hRac1 (mutant) + GSP <br />
**[[5hzh]], [[2wkp]], [[2wkq]], [[2wkr]] – hRac1 LOV2 domain (mutant) + GTP + MFN <br />
 
*Rac1 complex with protein
 
**[[5fi0]] – hRac1 + PTDINS (3,4,5)-dependent Rac exchanger <br />
**[[4yon]] – hRac1 (mutant) + PTDINS (3,4,5)-dependent Rac exchanger <br />
**[[2yin]] – hRac1 + dedicator of cytokinesis protein 2 <br />
**[[3b13]] – hRac1 (mutant) + dedicator of cytokinesis protein 2 <br />
**[[3bji]], [[2vrw]] – hRac1 + proto-oncogene VAV <br />
**[[2nz8]] – hRac1 + triple functional domain protein<br />
**[[1foe]] – hRac1 + TIAM1 <br />
 
*Rac1 complex with protein and nucleotide
 
**[[3ryt]] – hRac1 (mutant) + plexin-A1 + GNP<br />
**[[3su8]], [[3sua]] – hRac1 (mutant) + plexin-B1 + GNP<br />
**[[2rmk]] – hRac1 (mutant) + PRK1 + GCP - NMR<br />
**[[2fju]] – hRac1 + phospholipase C beta 2 + GSP <br />
**[[2h7v]] – hRac1 (mutant) + YpkA + GDP <br />
**[[1hh4]], [[1ds6]] – hRac1 + RhoGD1 + GDP <br />
**[[1i4d]], [[1i4l]] – hRac1 + arfaptin + GDP <br />
**[[1i4t]] – hRac1 + arfaptin + GNP <br />
**[[1g4u]] – hRac1 (mutant) + SPTP + GDP <br />
**[[1he1]] – hRac1 + GTPase-activating protein + GDP <br />
**[[1e96]] – hRac1 (mutant) + neutrophil cytosol factor 2 + GTP <br />
 
*Rac2
 
**[[2w2t]] – hRac2 (mutant) + GDP <br />
**[[2w2v]] – hRac2 (mutant) + GDTP <br />
**[[2w2x]] – hRac2 (mutant) + PLCG2 + GSP <br />
 
*Rac3


**[[2qme]] – hRac3 + PAK1 + GCP <br />
**[[2ov2]] – hRac3 + PAK4 + GCP <br />
**[[2ic5]] – hRac3 + GDP + GNP <br />
**[[2g0n]], [[2c2h]] – hRac3 + GDP  <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

Latest revision as of 12:51, 4 August 2024


Function

The small G-protein Rac or Ras-related C3 botulinum toxin substrate.

  • Rac1 is involved in the regulation of cytoskeletal organization, cell adhesion, migration and morphological changes[1].
  • Rac2 is expressed in hematopoietic cells exclusively[2].
  • Rac3 binds to a variety of effector proteins to regulate cellular responses like cell spreading and the formation of actin-based protrusions.

Disease

Mutations in Rac2 are associated with neutrophil immunodeficiency syndrome.

Structural highlights

The interactions between Rac1 and YpkA are via [3]. .

3D structures of Rac

Rac 3D structures


Human Rac1 (magenta) complex with YpkA (cyan), GDP and Mg+2 ion (green) (PDB code 2h7v)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Asahara S, Shibutani Y, Teruyama K, Inoue HY, Kawada Y, Etoh H, Matsuda T, Kimura-Koyanagi M, Hashimoto N, Sakahara M, Fujimoto W, Takahashi H, Ueda S, Hosooka T, Satoh T, Inoue H, Matsumoto M, Aiba A, Kasuga M, Kido Y. Ras-related C3 botulinum toxin substrate 1 (RAC1) regulates glucose-stimulated insulin secretion via modulation of F-actin. Diabetologia. 2013 May;56(5):1088-97. doi: 10.1007/s00125-013-2849-5. Epub 2013, Feb 15. PMID:23412604 doi:http://dx.doi.org/10.1007/s00125-013-2849-5
  2. ↑ Lougaris V, Baronio M, Gazzurelli L, Benvenuto A, Plebani A. RAC2 and primary human immune deficiencies. J Leukoc Biol. 2020 Aug;108(2):687-696. PMID:32542921 doi:10.1002/JLB.5MR0520-194RR
  3. ↑ Prehna G, Ivanov MI, Bliska JB, Stebbins CE. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell. 2006 Sep 8;126(5):869-80. PMID:16959567 doi:10.1016/j.cell.2006.06.056

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=Rac&oldid=4209053"