7yfv: Difference between revisions

Latest revision as of 19:47, 29 May 2024

Structure of Rpgrip1l CC1

Structural highlights

7yfv is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FTM_MOUSE Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R) (By similarity). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis (By similarity). Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins (PubMed:22927466). Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2 (PubMed:26150391).[UniProtKB:Q68CZ1]^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Rpgrip1l is one of the key ciliary proteins located at the transition zone of the primary cilium, an important organelle for cells to sense the outer environment. Mutations in the RPGRIP1L gene are associated with various ciliopathies. Here, we focused on the N-terminal coiled-coil of Rpgrip1l. By comprehensive biochemical and structural characterizations, we demonstrated that the two predicted coiled-coil regions (CC12) located at Rpgrip1l N-terminus each can form a stable parallel dimer. We further showed that overexpression of Rpgrip1l CC12 in NIH/3T3 cells significantly shortened the length of primary cilia, and this effect depended on the dimer formation. In addition, we found that CC12 of the homolog protein Rpgrip1 in mouse and human were significantly different from Rpgrip1l. Finally, we confirmed that some disease-related mutations can alter the dimeric states of CC12 of Rpgrip1l or Rpgrip1, which might explain the pathogenic mechanisms.

Structure of the N-terminal coiled-coil domains of the ciliary protein Rpgrip1l.,He R, Chen G, Li Z, Li J iScience. 2023 Feb 21;26(3):106249. doi: 10.1016/j.isci.2023.106249. eCollection , 2023 Mar 17. PMID:36915689^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Peters T, Ausmeier K, Rüther U. Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) mouse mutation. Mamm Genome. 1999 Oct;10(10):983-6. PMID:10501967 doi:10.1007/s003359901144
↑ Peters T, Ausmeier K, Dildrop R, Rüther U. The mouse Fused toes (Ft) mutation is the result of a 1.6-Mb deletion including the entire Iroquois B gene cluster. Mamm Genome. 2002 Apr;13(4):186-8. PMID:11956760 doi:10.1007/s00335-001-2142-7
↑ Sang L, Miller JJ, Corbit KC, Giles RH, Brauer MJ, Otto EA, Baye LM, Wen X, Scales SJ, Kwong M, Huntzicker EG, Sfakianos MK, Sandoval W, Bazan JF, Kulkarni P, Garcia-Gonzalo FR, Seol AD, O'Toole JF, Held S, Reutter HM, Lane WS, Rafiq MA, Noor A, Ansar M, Devi AR, Sheffield VC, Slusarski DC, Vincent JB, Doherty DA, Hildebrandt F, Reiter JF, Jackson PK. Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways. Cell. 2011 May 13;145(4):513-28. PMID:21565611 doi:10.1016/j.cell.2011.04.019
↑ Mahuzier A, Gaudé HM, Grampa V, Anselme I, Silbermann F, Leroux-Berger M, Delacour D, Ezan J, Montcouquiol M, Saunier S, Schneider-Maunoury S, Vesque C. Dishevelled stabilization by the ciliopathy protein Rpgrip1l is essential for planar cell polarity. J Cell Biol. 2012 Sep 3;198(5):927-40. PMID:22927466 doi:10.1083/jcb.201111009
↑ Gerhardt C, Lier JM, Burmühl S, Struchtrup A, Deutschmann K, Vetter M, Leu T, Reeg S, Grune T, Rüther U. The transition zone protein Rpgrip1l regulates proteasomal activity at the primary cilium. J Cell Biol. 2015 Jul 6;210(1):115-33. PMID:26150391 doi:10.1083/jcb.201408060
↑ He R, Chen G, Li Z, Li J. Structure of the N-terminal coiled-coil domains of the ciliary protein Rpgrip1l. iScience. 2023 Feb 21;26(3):106249. PMID:36915689 doi:10.1016/j.isci.2023.106249

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OCA

[1] Peters T, Ausmeier K, Rüther U. Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) mouse mutation. Mamm Genome. 1999 Oct;10(10):983-6. PMID:10501967 doi:10.1007/s003359901144

[2] Peters T, Ausmeier K, Dildrop R, Rüther U. The mouse Fused toes (Ft) mutation is the result of a 1.6-Mb deletion including the entire Iroquois B gene cluster. Mamm Genome. 2002 Apr;13(4):186-8. PMID:11956760 doi:10.1007/s00335-001-2142-7

[3] Sang L, Miller JJ, Corbit KC, Giles RH, Brauer MJ, Otto EA, Baye LM, Wen X, Scales SJ, Kwong M, Huntzicker EG, Sfakianos MK, Sandoval W, Bazan JF, Kulkarni P, Garcia-Gonzalo FR, Seol AD, O'Toole JF, Held S, Reutter HM, Lane WS, Rafiq MA, Noor A, Ansar M, Devi AR, Sheffield VC, Slusarski DC, Vincent JB, Doherty DA, Hildebrandt F, Reiter JF, Jackson PK. Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways. Cell. 2011 May 13;145(4):513-28. PMID:21565611 doi:10.1016/j.cell.2011.04.019

[4] Mahuzier A, Gaudé HM, Grampa V, Anselme I, Silbermann F, Leroux-Berger M, Delacour D, Ezan J, Montcouquiol M, Saunier S, Schneider-Maunoury S, Vesque C. Dishevelled stabilization by the ciliopathy protein Rpgrip1l is essential for planar cell polarity. J Cell Biol. 2012 Sep 3;198(5):927-40. PMID:22927466 doi:10.1083/jcb.201111009

[5] Gerhardt C, Lier JM, Burmühl S, Struchtrup A, Deutschmann K, Vetter M, Leu T, Reeg S, Grune T, Rüther U. The transition zone protein Rpgrip1l regulates proteasomal activity at the primary cilium. J Cell Biol. 2015 Jul 6;210(1):115-33. PMID:26150391 doi:10.1083/jcb.201408060

[6] He R, Chen G, Li Z, Li J. Structure of the N-terminal coiled-coil domains of the ciliary protein Rpgrip1l. iScience. 2023 Feb 21;26(3):106249. PMID:36915689 doi:10.1016/j.isci.2023.106249

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[7yfv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YFV FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yfv OCA], [https://pdbe.org/7yfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yfv RCSB], [https://www.ebi.ac.uk/pdbsum/7yfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yfv ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yfv OCA], [https://pdbe.org/7yfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yfv RCSB], [https://www.ebi.ac.uk/pdbsum/7yfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yfv ProSAT]</span></td></tr>
 </table>
 == Function ==

7yfv: Difference between revisions

Latest revision as of 19:47, 29 May 2024

Structure of Rpgrip1l CC1

Structural highlights

Function

Publication Abstract from PubMed

References

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