Trafficking of phosphatidylinositol by phosphatidylinositol transfer proteins.

@article{Cockcroft2007TraffickingOP,
  title={Trafficking of phosphatidylinositol by phosphatidylinositol transfer proteins.},
  author={Shamshad Cockcroft},
  journal={Biochemical Society symposium},
  year={2007},
  volume={74},
  pages={
          259-71
        }
}
  • S. Cockcroft
  • Published 12 January 2007
  • Biology, Chemistry
  • Biochemical Society symposium
PtdIns is synthesized at the endoplasmic reticulum and its intracellular distribution to other organelles can be facilitated by lipid transfer proteins [PITPs (phosphatidylinositol transfer proteins)]. In this review, I summarize the current understanding of how PITPs are regulated by phosphorylation, how can they dock to membranes to exchange their lipid cargo and how cells use PITPs in signal transduction and membrane delivery. Mammalian PITPs, PITPalpha and PITPbeta, are paralogous genes… 
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It is proposed that PITPs are regulators of phosphoinositide pathways by recruitment to membranes through specific protein interactions to promote molecular exchange between closely opposed membranes i.e., at membrane contact sites.

Biochemical and biological functions of class I phosphatidylinositol transfer proteins.

Dynamics of Lipid Transfer by Phosphatidylinositol Transfer Proteins in Cells

To study PITP dynamics in intact cells, chemically targeted their C95 residue that, although non‐essential for lipid transfer, is buried within the phospholipid‐binding cavity, and so, its chemical modification prevents PtdIns binding because of steric hindrance.

Phosphatidylinositol- and phosphatidylcholine-transfer activity of PITPβ is essential for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum

It is demonstrated that the PtdIns and PtdCho exchange activity of PITPβ is essential for COPI-mediated retrograde transport from the Golgi to the ER.

The phosphatidylinositol transfer protein RdgBβ binds 14-3-3 via its unstructured C-terminus, whereas its lipid-binding domain interacts with the integral membrane protein ATRAP (angiotensin II type I receptor-associated protein).

It is suggested that RdgBβ executes its function following recruitment to membranes via its PITP domain and the C-terminal end of the protein could regulate entry to the hydrophobic cavity.

Molecular insights into conformational dynamics associated with the open-closed-phosphorylated states of PITPα

The study shows that the open state is highly dynamic and its transition to closed state would stabilize PITP α, and the impact of phosphorylation on the global conformation of PITPα is discussed.

The multiple roles of PtdIns(4)P – not just the precursor of PtdIns(4,5)P2

The aim of this Commentary is to describe the present knowledge of PtdIns(4)P metabolism and the molecular machineries that are directly regulated by Ptd insurance within and outside of the Golgi complex.

Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles.

Characterization of three human sec14p-like proteins: alpha-tocopherol transport activity and expression pattern in tissues.

Research paper Characterization of three human sec14p-like proteins: a-Tocopherol transport activity and expression pattern in tissues

It is shown that the three recombinant hTAP proteins associate with the Golgi apparatus and mitochondria, and enhance the in vitro transport of radioactively labeled a-tocopherol to mitochondria in the same order of magnitude as the human a-tropopherol transfer protein (a-TTP).

References

Genes to cells