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Function
Rabphilin (Rab) is known as a synaptic vesicle-associated protein involved in the regulation of exo- and endocytosis processes at presynaptic sites[1].
Relevance
Rab is a major auto antigen in lymphocytic infundibulo-neurohypophysitis (LINH). Antibodies to Rab may serve as a biomarker for the diagnosis of LINH[2].
Structural highlights
The 3D structure of the complex between RO and its substrate reticuline show the cofactor FAD having bicovalent attachment to RO His and Cys. The substrate reticuline is seen in the active site cavity interacting with FAD and numerous RO sidechains[3].
- ↑ Stanic J, Carta M, Eberini I, Pelucchi S, Marcello E, Genazzani AA, Racca C, Mulle C, Di Luca M, Gardoni F. Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex. Nat Commun. 2015 Dec 18;6:10181. doi: 10.1038/ncomms10181. PMID:26679993 doi:https://dx.doi.org/10.1038/ncomms10181
- ↑ Iwama S, Sugimura Y, Kiyota A, Kato T, Enomoto A, Suzuki H, Iwata N, Takeuchi S, Nakashima K, Takagi H, Izumida H, Ochiai H, Fujisawa H, Suga H, Arima H, Shimoyama Y, Takahashi M, Nishioka H, Ishikawa SE, Shimatsu A, Caturegli P, Oiso Y. Rabphilin-3A as a Targeted Autoantigen in Lymphocytic Infundibulo-neurohypophysitis. J Clin Endocrinol Metab. 2015 Jul;100(7):E946-54. doi: 10.1210/jc.2014-4209. Epub, 2015 Apr 28. PMID:25919460 doi:https://dx.doi.org/10.1210/jc.2014-4209
- ↑ Winkler A, Lyskowski A, Riedl S, Puhl M, Kutchan TM, Macheroux P, Gruber K. A concerted mechanism for berberine bridge enzyme. Nat Chem Biol. 2008 Dec;4(12):739-41. Epub 2008 Oct 26. PMID:18953357 doi:https://dx.doi.org/10.1038/nchembio.123
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