scholarly journals Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway

1991 ◽  
Vol 95 (1) ◽  
pp. 164-170 ◽  
Author(s):  
Werner R. Bernhard ◽  
Sharon Thoma ◽  
Jose Botella ◽  
Chris R. Somerville
Keyword(s):  
Cdna Clone ◽  
Secretory Pathway ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein

Molecular cloning of a cDNA clone for tobacco lipid transfer protein and expression of the functional protein in Escherichia coli

FEBS Letters ◽  
1992 ◽  
Vol 311 (2) ◽  
pp. 119-123 ◽  
Author(s):  
Chikara Masuta ◽  
Masahiro Furuno ◽  
Hideo Tanaka ◽  
Mitsuhiro Yamada ◽  
Akira Koiwai
Keyword(s):  
Escherichia Coli ◽  
Molecular Cloning ◽  
Cdna Clone ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Functional Protein ◽  
Transfer Protein

scholarly journals A distal effect of microsomal triglyceride transfer protein deficiency on the lysosomal recycling of CD1d

2007 ◽  
Vol 204 (4) ◽  
pp. 921-928 ◽  
Author(s):  
Yuval Sagiv ◽  
Li Bai ◽  
Datsen G. Wei ◽  
Reuven Agami ◽  
Paul B. Savage ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Lipid Transfer Protein ◽  
Microsomal Triglyceride Transfer Protein ◽  
Lipid Transfer ◽  
Mhc I ◽  
Transfer Protein ◽  
Lipid Antigen ◽  
Lipid Presentation ◽  
Antigen Presenting ◽  
Lipid Loading

Microsomal triglyceride transfer protein (MTP) is an endoplasmic reticulum (ER)–resident lipid transfer protein involved in the biosynthesis and lipid loading of apolipoprotein B. MTP was recently suggested to directly regulate the biosynthesis of the MHC I–like, lipid antigen presenting molecule CD1d, based on coprecipitation experiments and lipid loading assays. However, we found that the major impact of MTP deficiency occurred distal to the ER and Golgi compartments. Thus, although the rates of CD1d biosynthesis, glycosylation maturation, and internalization from the cell surface were preserved, the late but essential stage of recycling from lysosome to plasma membrane was profoundly impaired. Likewise, functional experiments indicated defects of CD1d-mediated lipid presentation in the lysosome but not in the secretory pathway. These intriguing findings suggest a novel, unexpected role of MTP at a late stage of CD1d trafficking in the lysosomal compartment.

scholarly journals Miro recruits VPS13D to mitochondria

2020 ◽  
Author(s):  
Andrés Guillén-Samander ◽  
Marianna Leonzino ◽  
Pietro De Camilli
Keyword(s):  
Secretory Pathway ◽  
Lipid Transfer Protein ◽  
Transport Proteins ◽  
Lipid Transport ◽  
Eukaryotic Cells ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Accessory Factor ◽  
Mitochondrial Motility ◽  
Higher Eukaryotes

AbstractMitochondria, which are excluded from the secretory pathway, depend on lipid transport proteins for their lipid supply from the ER, where most lipids are synthesized. In yeast, the outer membrane GTPase Gem1 is an accessory factor of ERMES, an ER-mitochondria tethering complex that contains lipid transport domains and plays a function, partially redundant with VPS13, in lipid transfer between the two organelles. In metazoa, where VPS13, but not ERMES, is present, the Gem1 orthologue Miro has been linked to mitochondrial motility but not to lipid transport. Here we show that Miro recruits to mitochondria the lipid transport protein VPS13D which, like Miro, is an essential protein in mammals, and whose localization had remained elusive. We also show that VPS13D can tether mitochondria to the ER in a Miro- and VAP-dependent way. These findings reveal a so far missing link between function(s) of Gem1/Miro in yeast and higher eukaryotes, where Miro is a Parkin substrate, with potential implications for Parkinson’s disease pathogenesis.SummaryProtein-mediated ER-mitochondria lipid transfer is critical for eukaryotic cells. However, the underlying machinery is not well conserved. Guillén-Samander et al, show that Gem1/Miro is an evolutionary conserved link between the yeast ERMES complex and the mammalian lipid transfer protein VPS13D.

The Oxysterol-Binding Protein Cycle: Burning Off PI(4)P to Transport Cholesterol

2018 ◽  
Vol 87 (1) ◽  
pp. 809-837 ◽  
Author(s):  
Bruno Antonny ◽  
Joëlle Bigay ◽  
Bruno Mesmin
Keyword(s):  
Secretory Pathway ◽  
Lipid Transfer Protein ◽  
Binding Protein ◽  
Asymmetric Distribution ◽  
Lipid Transfer ◽  
Oxysterol Binding Protein ◽  
Transfer Protein ◽  
Lipid Exchange ◽  
Opposite Process ◽  
Phosphatidylinositol 4

To maintain an asymmetric distribution of ions across membranes, protein pumps displace ions against their concentration gradient by using chemical energy. Here, we describe a functionally analogous but topologically opposite process that applies to the lipid transfer protein (LTP) oxysterol-binding protein (OSBP). This multidomain protein exchanges cholesterol for the phosphoinositide phosphatidylinositol 4-phosphate [PI(4)P] between two apposed membranes. Because of the subsequent hydrolysis of PI(4)P, this counterexchange is irreversible and contributes to the establishment of a cholesterol gradient along organelles of the secretory pathway. The facts that some natural anti-cancer molecules block OSBP and that many viruses hijack the OSBP cycle for the formation of intracellular replication organelles highlight the importance and potency of OSBP-mediated lipid exchange. The architecture of some LTPs is similar to that of OSBP, suggesting that the principles of the OSBP cycle—burning PI(4)P for the vectorial transfer of another lipid—might be general.

scholarly journals The key to the allergenicity of lipid transfer protein (LTP) ligands: A structural characterization

2021 ◽  
pp. 158928
Author(s):  
Zulema Gonzalez-Klein ◽  
Bruno Cuevas-Zuviria ◽  
Andrea Wangorsch ◽  
Guadalupe Hernandez-Ramirez ◽  
Diego Pazos-Castro ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein
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