Cullin: Difference between revisions

Latest revision as of 10:10, 20 May 2019

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Human cullin-1 (cyan) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code 1ldj)

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Cullins are hydrophobic scaffold proteins for E3 ubiquitin ligases. They combine with ring box proteins (RBX) to form the CRL complex.^[1] The CRL complex is essential in targeting proteins to ubiquitin-mediated destruction. Cullin-1 to 7 are part of the multi-subunit ubiquitin complex. Conjugation of cullin to NEDD8 modulates the activation of the CRL.

Cullin-1 is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.^[2]
Cullin-2 is part of the ECS (Elongin-cullin-SOCS-box) complex.^[3]
Cullin-3 is part of the BTB-Cul3 complex.^[4]
Cullin-4A and 4B regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.^[5]
Cullin-5 inhibits cellular proliferation.^[6]
Cullin-7 is a core component of a complex which mediates ubiquitination of target proteins.^[7]

Human cullin-1 complex with ring box protein 1 and Zn+2 ions.

1st Zn coordination site.

2nd Zn coordination site.

3rd Zn coordination site.(PDB code 1ldj)

3D Structures of cullin

Cullin 3D structures

↑ Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol. 2005 Jan;6(1):9-20. PMID:15688063 doi:https://dx.doi.org/10.1038/nrm1547
↑ Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature. 2002 Apr 18;416(6882):703-9. PMID:11961546 doi:https://dx.doi.org/10.1038/416703a
↑ Nguyen HC, Yang H, Fribourgh JL, Wolfe LS, Xiong Y. Insights into Cullin-RING E3 Ubiquitin Ligase Recruitment: Structure of the VHL-EloBC-Cul2 Complex. Structure. 2015 Feb 3. pii: S0969-2126(14)00423-7. doi:, 10.1016/j.str.2014.12.014. PMID:25661653 doi:https://dx.doi.org/10.1016/j.str.2014.12.014
↑ Canning P, Cooper CD, Krojer T, Murray JW, Pike AC, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock AN. Structural basis for Cul3 assembly with the BTB-Kelch family of E3 ubiquitin ligases. J Biol Chem. 2013 Jan 24. PMID:23349464 doi:https://dx.doi.org/10.1074/jbc.M112.437996
↑ Fischer ES, Scrima A, Bohm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thoma NH. The Molecular Basis of CRL4(DDB2/CSA) Ubiquitin Ligase Architecture, Targeting, and Activation. Cell. 2011 Nov 23;147(5):1024-39. PMID:22118460 doi:10.1016/j.cell.2011.10.035
↑ Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell. 2008 Sep 19;134(6):995-1006. PMID:18805092 doi:https://dx.doi.org/10.1016/j.cell.2008.07.022
↑ Kaustov L, Lukin J, Lemak A, Duan S, Ho M, Doherty R, Penn LZ, Arrowsmith CH. The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53. J Biol Chem. 2007 Apr 13;282(15):11300-7. Epub 2007 Feb 12. PMID:17298945 doi:10.1074/jbc.M611297200

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol. 2005 Jan;6(1):9-20. PMID:15688063 doi:https://dx.doi.org/10.1038/nrm1547

[2] Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature. 2002 Apr 18;416(6882):703-9. PMID:11961546 doi:https://dx.doi.org/10.1038/416703a

[3] Nguyen HC, Yang H, Fribourgh JL, Wolfe LS, Xiong Y. Insights into Cullin-RING E3 Ubiquitin Ligase Recruitment: Structure of the VHL-EloBC-Cul2 Complex. Structure. 2015 Feb 3. pii: S0969-2126(14)00423-7. doi:, 10.1016/j.str.2014.12.014. PMID:25661653 doi:https://dx.doi.org/10.1016/j.str.2014.12.014

[4] Canning P, Cooper CD, Krojer T, Murray JW, Pike AC, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock AN. Structural basis for Cul3 assembly with the BTB-Kelch family of E3 ubiquitin ligases. J Biol Chem. 2013 Jan 24. PMID:23349464 doi:https://dx.doi.org/10.1074/jbc.M112.437996

[5] Fischer ES, Scrima A, Bohm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thoma NH. The Molecular Basis of CRL4(DDB2/CSA) Ubiquitin Ligase Architecture, Targeting, and Activation. Cell. 2011 Nov 23;147(5):1024-39. PMID:22118460 doi:10.1016/j.cell.2011.10.035

[6] Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell. 2008 Sep 19;134(6):995-1006. PMID:18805092 doi:https://dx.doi.org/10.1016/j.cell.2008.07.022

[7] Kaustov L, Lukin J, Lemak A, Duan S, Ho M, Doherty R, Penn LZ, Arrowsmith CH. The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53. J Biol Chem. 2007 Apr 13;282(15):11300-7. Epub 2007 Feb 12. PMID:17298945 doi:10.1074/jbc.M611297200

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@@ Line 1: / Line 1: @@
-<StructureSection load='1ldj' size='340' side='right' caption='Human cullin-1 (grey) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code [[1ldj]])' scene=''>
+<StructureSection load='' size='340' side='right' caption='Human cullin-1 (cyan) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code [[1ldj]])' scene='70/706699/Cv/2'>
 '''Cullins''' are hydrophobic scaffold proteins for E3 ubiquitin ligases.  They combine with ring box proteins (RBX) to form the CRL complex.<ref>PMID:15688063</ref>  The CRL complex is essential in targeting proteins to ubiquitin-mediated destruction.  Cullin-1 to 7 are part of the multi-subunit ubiquitin complex.  Conjugation of cullin to NEDD8 modulates the activation of the CRL.<br />
-*'''Cullin-1''' is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.<br />
+*'''Cullin-1''' is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.<ref>PMID:11961546</ref><br />
-*'''Cullin-2''' is part of the ECS (Elongin-cullin-SOCS-box) complex.<br />
+*'''Cullin-2''' is part of the ECS (Elongin-cullin-SOCS-box) complex.<ref>PMID:25661653</ref><br />
-*'''Cullin-3''' is part of the BTB-Cul3 complex. <br />
+*'''Cullin-3''' is part of the BTB-Cul3 complex.<ref>PMID:23349464</ref> <br />
-*'''Cullin-4A and 4B''' regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.<br />
+*'''Cullin-4A and 4B''' regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.<ref>PMID:22118460</ref><br />
-*'''Cullin-5''' inhibits cellular proliferation.<br />
+*'''Cullin-5''' inhibits cellular proliferation.<ref>PMID:18805092</ref><br />
+*'''Cullin-7''' is a core component of a complex which mediates ubiquitination of target proteins.<ref>PMID:17298945</ref><br />
-</StructureSection>
+<scene name='70/706699/Cv/7'>Human cullin-1 complex with ring box protein 1 and Zn+2 ions</scene>.
-== 3D Structures of cullin==
+<scene name='70/706699/Cv/8'>1st Zn coordination site</scene>.
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+<scene name='70/706699/Cv/9'>2nd Zn coordination site</scene>.
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Cullin-1
+<scene name='70/706699/Cv/10'>3rd Zn coordination site</scene>.(PDB code [[1ldj]])
-**[[1ldj]] – hCul1 + RBX1 – human <br />
+== 3D Structures of cullin==
-**[[3rtr]] – hCul1 residues 411-766 (mutant) + RBX1  <br />
+[[Cullin 3D structures]]
-**[[3tdu]] – hCul1 residues 702-776 + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12  <br />
-**[[3tdz]] – hCul1 residues 702-776 + Dcn1-like protein + stapled Ubc12 peptide <br />
-**[[1ldk]] – hCul1 + RBX1 + cyclin A/Cdk2-asociated protein + Skp2-like protein <br />
-**[[1u6g]] – hCul1 + RBX1 + TIP120 protein  <br />
-**[[4f52]] – hCul1 residues 411-690 (mutant) + RBX1 + glomulin<br />
-**[[4p5o]] – hCul1 residues 411-776 + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12 + RBX1 +  NEDD8-conjugating enzyme Ubc12 + NEDD8 <br />
-*Cullin-2
+</StructureSection>
-**[[4wqo]] – hCul2 residues 20-122 + PVHL + transcription elongation factor B <br />
-*Cullin-3
-**[[4ap2]], [[4apf]], [[4hxi]] – hCul3 N terminal (mutant) + kelch-like protein  <br />
-**[[4eoz]] – hCul3 N terminal (mutant) + peckle-type POZ protein  <br />
-**[[2myl]], [[2mym]] – hCul3 residues 49-68 - NMR <br />
-*Cullin-4A
-**[[2hye]] – hCul4A + RBX1 + DNA damage-binding protein 1 + nonstructural protein <br />
-**[[4a0k]] – hCul4A + RBX1 + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA<br />
-*Cullin-4B
-**[[4a64]] – hCul4B residues 188-539 <br />
-**[[2do7]] – hCul4B winged helix-turn-helix - NMR <br />
-**[[4a0c]] – hCul4B residues 192-913 + RBX1 + cullin-associated NEDD8-dissociated protein <br />
-**[[4a0l]] – hCul4B + RBX1 + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA<br />
-*Cullin-5
-**[[2wzk]] – hCul5 N terminal (mutant) <br />
-**[[3dpl]] – hCul5 residues 401-780 (mutant) + RBX1  <br />
-**[[3dqv]] – hCul5 residues 401-780 (mutant) + RBX1 + NEDD8 <br />
-**[[4jgh]] – hCul5 N terminal (mutant) + SOCS-2 + transcription elongation factor B <br />
-**[[4n9f]] – hCul5 N terminal + core-binding factor + virion infectivity factor + transcription elongation factor B <br />
-*Cullin-7
-**[[2jng]] – hCul7 residues 360-460 - NMR <br />
-*Cullin-A
-**[[3o2p]], [[3o6b]] – CulA residues 730-815 + defective in cullin neddylation protein - yeast
-}}
 == References ==
 <references/>
+[[Category:Topic Page]]

Cullin: Difference between revisions

Latest revision as of 10:10, 20 May 2019

3D Structures of cullin

References

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