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© 2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.

Abstract

ACBD3 inhibited SREBP1-sensitive promoter activity of fatty acid synthase (FASN). [...]ACBD3 blocked intracellular maturation of SREBP1 probably through directly binding with the lipid regulator rather than disrupting SREBP1–SCAP–Insig1 interaction. Since ACBD3 is important in maintaining the integrity of Golgi morphology, these data also establish the importance of the Golgi complex for the transfer of GlcCer and complex GSL synthesis. 5. [...]GRASP55, a well-known Golgin45-binding partner and Golgi stacking protein, was also selectively enriched in the Golgin45–ACBD3–TBC1D22 complex. [...]this large multi-protein complex (GRASP55–Golgin45–ACBD3–TBC1D22) seems to form a membrane micro-domain between the medial-Golgi cisternae and contributes to membrane trafficking and Golgi structure maintenance. ACBD3 in Iron Uptake At the mitochondria, stimulation of NMDAR (N-methyl-D-aspartate receptor) leads to activation of nNOS (neuron nitric oxide synthase), which generates NO (nitric oxide) and activates Dextras1 (dexamethasone-induced Ras-related protein 1) by its S-nitrosylation on cysteine 11, and results in iron uptake through Dextras1′s binding proteins, PAP7 and DMT1 (the divalent metal transporter 1) [18,38].

Details

Title
Acyl-CoA-Binding Domain-Containing 3 (ACBD3; PAP7; GCP60): A Multi-Functional Membrane Domain Organizer
Author
Yue, Xihua; Qian, Yi; Gim, Bopil; Lee, Intaek
Publication year
2019
Publication date
2019
Publisher
MDPI AG
ISSN
16616596
e-ISSN
14220067
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2332335012
Copyright
© 2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.