Macromolecular assemblies regulate non-vesicular phosphatidylserine traffic in yeast

J. Y. Choi, W. R. Riekhof, W. I. Wu, D. R. Voelker

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

PtdSer (phosphatidylserine) is synthesized in the endoplasmic reticulum and the related MAM (mitochondria-associated membrane), and transported to the PtdSer decarboxylases, Pds1p in the mitochondria, and Psd2p in the Golgi. Genetic and biochemical analyses of PtdSer transport are now revealing the role of specific protein and lipid assemblies on different organelles that regulate non-vesicular PtdSer transport. The transport of PtdSer from MAM to mitochondria is regulated by at least three genes: MET30 (encoding a ubiquitin ligase), MET4 (encoding a transcription factor), and one or more unknown genes whose transcription is regulated by MET4. MET30-dependent ubiquitination is required for the MAM to function as a competent donor membrane and for the mitochondria to function as a competent acceptor membrane. Non-vesicular transport of PtdSer to the locus of Psd2p is under the control of at least three genes, STT4 [encoding Stt4p (phosphatidylinositol 4-kinase)], PSTB2 (encoding the lipid-binding protein PstB2p) and PSD2 (encoding Psd2p). Stt4p is proposed to produce a pool of Ptdlns4P that is necessary for lipid transport. PstB2p and Psd2p must be present on the acceptor membrane for PtdSer transport to occur. Psd2p contains a C2 (Ca2+ and phospholipid binding sequence) domain that is required for lipid transport. Reconstitution studies with chemically defined donor membranes demonstrate that membrane domains rich in the anionic lipids, PtdSer, Ptdlns4P and phosphatidic acid function as the most efficient donors of PtdSer to Psd2p. The emerging view is that macromolecular complexes dependent on protein-protein and protein-lipid interactions form between donor and acceptor membranes and serve to dock the compartments and facilitate phospholipid transport.

Original languageEnglish (US)
Pages (from-to)404-408
Number of pages5
JournalBiochemical Society Transactions
Volume34
Issue number3
DOIs
StatePublished - Jun 1 2006

Fingerprint

Phosphatidylserines
Yeast
Mitochondria
Yeasts
Membranes
Lipids
Gene encoding
Phospholipids
Proteins
Genes
Macromolecular Substances
Phosphatidic Acids
Docks
1-Phosphatidylinositol 4-Kinase
Ubiquitination
Transcription
Ligases
Ubiquitin
Endoplasmic Reticulum
Organelles

Keywords

  • Endoplasmic reticulum
  • Macromolecular assembly
  • Mitochondria-associated membrane (MAM)
  • Phosphatidylserine traffic
  • Ubiquitination
  • Yeast

ASJC Scopus subject areas

  • Biochemistry

Cite this

Macromolecular assemblies regulate non-vesicular phosphatidylserine traffic in yeast. / Choi, J. Y.; Riekhof, W. R.; Wu, W. I.; Voelker, D. R.

In: Biochemical Society Transactions, Vol. 34, No. 3, 01.06.2006, p. 404-408.

Research output: Contribution to journalArticle

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