Phosphatidylinositol transfer proteins: From closed for transport to open for exchange

Wirtz, K.W.A.; Schouten, Arie; Gros, Piet

doi:10.1016/j.advenzreg.2006.01.020

Cited by 17 publications

(13 citation statements)

References 31 publications

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“…Phosphatidylinositol transfer proteins (PITP) are ubiquitous in all mammalian tissues and highly conserved (> 98% identity) [22]. The primary member of this family, PITPα, is a multifunctional protein with regulatory roles in intracellular lipid and vesicular trafficking and in lipid-mediated signal transduction pathways.…”

Section: Resultsmentioning

confidence: 99%

“…Despite no significant sequence homology, the PRELI-like domain shows a remote structural similarity to other lipid-binding proteins including the phosphatidylinositol transfer proteins (PITPs) [22] and the related cholesterol-binding START domains [23]. Phosphatidylinositol transfer proteins (PITP) are ubiquitous in all mammalian tissues and highly conserved (> 98% identity) [22]. The primary member of this family, PITPa, is a multifunctional protein with regulatory roles in intracellular lipid and vesicular trafficking and in lipid-mediated signal transduction pathways.…”

Section: The Preli-like Domain Of Slmo1 Resembles Mammalian Phosphatimentioning

confidence: 99%

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Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

et al. 2015

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The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1–SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.

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Section: Resultsmentioning

confidence: 99%

Section: The Preli-like Domain Of Slmo1 Resembles Mammalian Phosphatimentioning

confidence: 99%

Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

et al. 2015

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“…4B) (Im et al 2005;Wirtz et al 2006). In the closed conformation the lid is often stabilized by hydrogen bonds and hydrophobic interactions with the rest of the protein.…”

Section: Nonvesicular Lipid Transport By Ltpsmentioning

confidence: 99%

“…4B). Typically, a "lid" covers the hydrophobic tunnel and acts as a gate for lipid uptake and release (Im et al 2005;Wirtz et al 2006). The interaction of an LTP with membranes is thought to induce conformational changes, leading to displacement of the lid from the lipid-binding cavity and, consequently, tunnel opening (Lev 2010).…”

Section: Nonvesicular Lipid Transport By Ltpsmentioning

confidence: 99%

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Lev

2012

Cold Spring Harbor Perspectives in Biology

103

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“…It is linked to cell proliferation and cell cycle control but also mediates apoptosis in rat pituitary tumour cells in response to thyroid hormone [56]. The phosphatidylinositol transfer protein, Pitpn, regulates intracellular transfer of phospholipids and the activity of phosphatidylinositol signalling pathways [57], [58].…”

Section: Discussionmentioning

confidence: 99%

Genomic Analysis of the Function of the Transcription Factor gata3 during Development of the Mammalian Inner Ear

Milo

Cacciabue-Rivolta²,

Kneebone³

et al. 2009

PLoS ONE

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We have studied the function of the zinc finger transcription factor gata3 in auditory system development by analysing temporal profiles of gene expression during differentiation of conditionally immortal cell lines derived to model specific auditory cell types and developmental stages. We tested and applied a novel probabilistic method called the gamma Model for Oligonucleotide Signals to analyse hybridization signals from Affymetrix oligonucleotide arrays. Expression levels estimated by this method correlated closely (p<0.0001) across a 10-fold range with those measured by quantitative RT-PCR for a sample of 61 different genes. In an unbiased list of 26 genes whose temporal profiles clustered most closely with that of gata3 in all cell lines, 10 were linked to Insulin-like Growth Factor signalling, including the serine/threonine kinase Akt/PKB. Knock-down of gata3 in vitro was associated with a decrease in expression of genes linked to IGF-signalling, including IGF1, IGF2 and several IGF-binding proteins. It also led to a small decrease in protein levels of the serine-threonine kinase Akt2/PKBβ, a dramatic increase in Akt1/PKBα protein and relocation of Akt1/PKBα from the nucleus to the cytoplasm. The cyclin-dependent kinase inhibitor p27kip1, a known target of PKB/Akt, simultaneously decreased. In heterozygous gata3 null mice the expression of gata3 correlated with high levels of activated Akt/PKB. This functional relationship could explain the diverse function of gata3 during development, the hearing loss associated with gata3 heterozygous null mice and the broader symptoms of human patients with Hearing-Deafness-Renal anomaly syndrome.

show abstract

Phosphatidylinositol transfer proteins: From closed for transport to open for exchange

Cited by 17 publications

References 31 publications

Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Genomic Analysis of the Function of the Transcription Factor gata3 during Development of the Mammalian Inner Ear

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