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Characterization of the Arabidopsis thaliana glycosphingolipid transfer protein GLTP1 by Gun West; Johan Edqvist; Peter Mattjus is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## S55 by PtdSer decarboxylase 1(Psd1p) cannot be replaced by PtdEtn generated by the Kennedy pathway or Psd2p in the Golgi. The depleted mitochondrial pool of PtdEtn, occurring in cells devoid of Psd1p, is restored by supplementing cells with lyso-PtdEtn. Lyso-PtdEtn is efficiently transported into cells by the aminophospholipid transporters, Dnf1p and Dnf2p, and their regulatory subunit Lem3p. Lyso-PtdEtn is acylated by Ale1p to form PtdEtn and can fulfill all the cellular requirements for PtdEtn and PtdCho. PtdEtn synthesis in the Golgi by Psd2p requires transport of PtdSer from the ER. Genetic and biochemical studies demonstrate the transport of PtdSer to Psd2p requires the function of the PtdIns-4-kinase, Stt4p, and an anionic phospholipid binding protein PstB2p. Psd2p participates in the transport reaction via protein-lipid interactions involving its C2 domains. Two hybrid analyses reveal that Psd2p directly interacts with PstB2p. PstB2p also interacts with its cognate binding protein named Pbi1p, which in turn can bind to an integral ER tethering protein Scs2p. Thus, PtdSer transport to the Golgi occurs via assemblies of proteins and lipids that form between this organelle a

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Author

Gun West; Johan Edqvist; Peter Mattjus

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0009-3084)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)