De Camilli P - Search Results

1

Role of VPS13, a protein with similarity to ATG2, in physiology and disease.

Ugur B, Hancock-Cerutti W, Leonzino M, De Camilli P. Ugur B, et al. Among authors: de camilli p. Curr Opin Genet Dev. 2020 Dec;65:61-68. doi: 10.1016/j.gde.2020.05.027. Epub 2020 Jun 18. Curr Opin Genet Dev. 2020. PMID: 32563856 Free PMC article. Review.

2

VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites.

Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P. Kumar N, et al. Among authors: de camilli p. J Cell Biol. 2018 Oct 1;217(10):3625-3639. doi: 10.1083/jcb.201807019. Epub 2018 Aug 9. J Cell Biol. 2018. PMID: 30093493 Free PMC article.

3

VPS13D bridges the ER to mitochondria and peroxisomes via Miro.

Guillén-Samander A, Leonzino M, Hanna MG, Tang N, Shen H, De Camilli P. Guillén-Samander A, et al. Among authors: de camilli p. J Cell Biol. 2021 May 3;220(5):e202010004. doi: 10.1083/jcb.202010004. J Cell Biol. 2021. PMID: 33891013 Free PMC article.

4

Correction: VPS13D bridges the ER to mitochondria and peroxisomes via Miro.

Guillén-Samander A, Leonzino M, Hanna MG, Tang N, Shen H, De Camilli P. Guillén-Samander A, et al. Among authors: de camilli p. J Cell Biol. 2021 Aug 2;220(8):e20201000405052021c. doi: 10.1083/jcb.20201000405052021c. Epub 2021 Jun 22. J Cell Biol. 2021. PMID: 34156432 Free PMC article. No abstract available.

5

Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport.

Leonzino M, Reinisch KM, De Camilli P. Leonzino M, et al. Among authors: de camilli p. Biochim Biophys Acta Mol Cell Biol Lipids. 2021 Oct;1866(10):159003. doi: 10.1016/j.bbalip.2021.159003. Epub 2021 Jul 1. Biochim Biophys Acta Mol Cell Biol Lipids. 2021. PMID: 34216812 Free PMC article. Review.

6

ER-lysosome lipid transfer protein VPS13C/PARK23 prevents aberrant mtDNA-dependent STING signaling.

Hancock-Cerutti W, Wu Z, Xu P, Yadavalli N, Leonzino M, Tharkeshwar AK, Ferguson SM, Shadel GS, De Camilli P. Hancock-Cerutti W, et al. Among authors: de camilli p. J Cell Biol. 2022 Jul 4;221(7):e202106046. doi: 10.1083/jcb.202106046. Epub 2022 Jun 3. J Cell Biol. 2022. PMID: 35657605 Free PMC article.

7

In situ architecture of the lipid transport protein VPS13C at ER-lysosome membrane contacts.

Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. Cai S, et al. Among authors: de camilli p. Proc Natl Acad Sci U S A. 2022 Jul 19;119(29):e2203769119. doi: 10.1073/pnas.2203769119. Epub 2022 Jul 13. Proc Natl Acad Sci U S A. 2022. PMID: 35858323 Free PMC article.

8

A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane.

Guillén-Samander A, Wu Y, Pineda SS, García FJ, Eisen JN, Leonzino M, Ugur B, Kellis M, Heiman M, De Camilli P. Guillén-Samander A, et al. Among authors: de camilli p. Proc Natl Acad Sci U S A. 2022 Aug 30;119(35):e2205425119. doi: 10.1073/pnas.2205425119. Epub 2022 Aug 22. Proc Natl Acad Sci U S A. 2022. PMID: 35994651 Free PMC article.

9

VPS13B is localized at the cis-trans Golgi complex interface and is a functional partner of FAM177A1.

Ugur B, Schueder F, Shin J, Hanna MG, Wu Y, Leonzino M, Su M, McAdow AR, Wilson C, Postlethwait J, Solnica-Krezel L, Bewersdorf J, De Camilli P. Ugur B, et al. Among authors: de camilli p. bioRxiv [Preprint]. 2023 Dec 18:2023.12.18.572081. doi: 10.1101/2023.12.18.572081. bioRxiv. 2023. Update in: J Cell Biol. 2024 Dec 2;223(12):e202311189. doi: 10.1083/jcb.202311189 PMID: 38187698 Free PMC article. Updated. Preprint.

10

Lysosome damage triggers acute formation of ER to lysosomes membrane tethers mediated by the bridge-like lipid transport protein VPS13C.

Wang X, Xu P, Bentley-DeSousa A, Hancock-Cerutti W, Cai S, Johnson BT, Tonelli F, Talaia G, Alessi DR, Ferguson SM, De Camilli P. Wang X, et al. Among authors: de camilli p. bioRxiv [Preprint]. 2024 Jun 8:2024.06.08.598070. doi: 10.1101/2024.06.08.598070. bioRxiv. 2024. PMID: 38895395 Free PMC article. Preprint.

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