7q3e

Structure of the mouse CPLANE-RSG1 complexStructure of the mouse CPLANE-RSG1 complex

Structural highlights

7q3e 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:	Electron Microscopy, Resolution 3.35Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FRITZ_MOUSE Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (PubMed:27158779).[UniProtKB:Q32NR9]^[1]

Publication Abstract from PubMed

Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ciliogenesis and planar polarity effector (CPLANE) proteins Wdpcp, Inturned, and Fuzzy. CPLANE proteins are essential for building the cilium and are mutated in multiple ciliopathies, yet their structure and molecular functions remain elusive. Here, we show that mammalian CPLANE proteins comprise a bona fide complex and report the near-atomic resolution structures of the human Wdpcp-Inturned-Fuzzy complex and of the mouse Wdpcp-Inturned-Fuzzy complex bound to the small guanosine triphosphatase Rsg1. Notably, the crescent-shaped CPLANE complex binds phospholipids such as phosphatidylinositol 3-phosphate via multiple modules and a CPLANE ciliopathy mutant exhibits aberrant lipid binding. Our study provides critical structural and functional insights into an enigmatic ciliogenesis-associated complex as well as unexpected molecular rationales for ciliopathies.

Structure of the ciliogenesis-associated CPLANE complex.,Langousis G, Cavadini S, Boegholm N, Lorentzen E, Kempf G, Matthias P Sci Adv. 2022 Apr 15;8(15):eabn0832. doi: 10.1126/sciadv.abn0832. Epub 2022 Apr , 15. PMID:35427153^[2]

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

References

↑ Toriyama M, Lee C, Taylor SP, Duran I, Cohn DH, Bruel AL, Tabler JM, Drew K, Kelly MR, Kim S, Park TJ, Braun DA, Pierquin G, Biver A, Wagner K, Malfroot A, Panigrahi I, Franco B, Al-Lami HA, Yeung Y, Choi YJ, Duffourd Y, Faivre L, Rivière JB, Chen J, Liu KJ, Marcotte EM, Hildebrandt F, Thauvin-Robinet C, Krakow D, Jackson PK, Wallingford JB. The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery. Nat Genet. 2016 Jun;48(6):648-56. PMID:27158779 doi:10.1038/ng.3558
↑ Langousis G, Cavadini S, Boegholm N, Lorentzen E, Kempf G, Matthias P. Structure of the ciliogenesis-associated CPLANE complex. Sci Adv. 2022 Apr 15;8(15):eabn0832. PMID:35427153 doi:10.1126/sciadv.abn0832

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OCA

[1] Toriyama M, Lee C, Taylor SP, Duran I, Cohn DH, Bruel AL, Tabler JM, Drew K, Kelly MR, Kim S, Park TJ, Braun DA, Pierquin G, Biver A, Wagner K, Malfroot A, Panigrahi I, Franco B, Al-Lami HA, Yeung Y, Choi YJ, Duffourd Y, Faivre L, Rivière JB, Chen J, Liu KJ, Marcotte EM, Hildebrandt F, Thauvin-Robinet C, Krakow D, Jackson PK, Wallingford JB. The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery. Nat Genet. 2016 Jun;48(6):648-56. PMID:27158779 doi:10.1038/ng.3558

[2] Langousis G, Cavadini S, Boegholm N, Lorentzen E, Kempf G, Matthias P. Structure of the ciliogenesis-associated CPLANE complex. Sci Adv. 2022 Apr 15;8(15):eabn0832. PMID:35427153 doi:10.1126/sciadv.abn0832

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