scholarly journals Thank ORP9 for FFAT: With endosomal ORP10, it’s fission accomplished!

2021 ◽  
Vol 221 (1) ◽  
Author(s):  
Louise H. Wong ◽  
Andrea Martello ◽  
Emily R. Eden
Keyword(s):  
Membrane Phospholipid ◽  
Endocytic Trafficking ◽  
Phospholipid Content ◽  
Endosomal Membrane ◽  
Contact Sites

Heterogeneity in endosomal membrane phospholipid content is emerging as a regulator of endocytic trafficking pathways. Kawasaki et al. (2021. J. Cell. Biol.https://doi.org/10.1083/jcb.202103141) demonstrate exchange of endosomal PI4P for PS by ORP10 at ER–endosome contact sites, with the consequent recruitment of endosomal fission factors.

Study on the relationship of cPLA2, CK-MB, and membrane phospholipid content in acute myocardial infarction

2010 ◽  
Vol 26 (1) ◽  
pp. 64-68 ◽  
Author(s):  
Li Wei-hua ◽  
Han Jun-yu ◽  
Sun Chang-qing ◽  
Guo Yong-jun ◽  
Xie Qiang ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Membrane Phospholipid ◽  
Phospholipid Content ◽  
Relationship Of ◽  
The Relationship

scholarly journals Daptomycin Resistance in Enterococci Is Associated with Distinct Alterations of Cell Membrane Phospholipid Content

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e43958 ◽  
Author(s):  
Nagendra N. Mishra ◽  
Arnold S. Bayer ◽  
Truc T. Tran ◽  
Yousif Shamoo ◽  
Eugenia Mileykovskaya ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Phospholipid ◽  
Phospholipid Content

Selective Effect of a Diet-Induced Decrease in the Arachidonic Acid Membrane-Phospholipid Content on in vitro Phospholipase C and Adenylate Cyclase-Mediated Pituitary Response to Angiotensin II

1994 ◽  
Vol 60 (4) ◽  
pp. 400-409 ◽  
Author(s):  
Maria Luiza Aléssio ◽  
Claude Louis Léger ◽  
Ramahefarizo Rasolonjanahary ◽  
Dolores E. Wandscheer ◽  
Hubert Clauser ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Angiotensin Ii ◽  
Adenylate Cyclase ◽  
Phospholipase C ◽  
Membrane Phospholipid ◽  
Phospholipid Content ◽  
Selective Effect

Analysis of the dual function of the ESCRT-III protein Snf7 in endocytic trafficking and in gene expression

2009 ◽  
Vol 424 (1) ◽  
pp. 89-97 ◽  
Author(s):  
Peter Weiss ◽  
Stefanie Huppert ◽  
Ralf Kölling
Keyword(s):  
Endocytic Trafficking ◽  
Dual Function ◽  
Alkaline Ph ◽  
Endosomal Sorting ◽  
Endosomal Membrane ◽  
Binding Partners ◽  
Interaction Partners ◽  
Pathway Function ◽  
Multivesicular Endosomes ◽  
Additional Role

ESCRT (endosomal sorting complex required for transport)-III mediates the budding and scission of intralumenal vesicles into multivesicular endosomes in yeast. For the main ESCRT-III subunit Snf7, an additional role in activation of the transcription factor Rim101 (the ‘Rim pathway’) is now also firmly established. In the present study, we investigate how these two Snf7 functions are related to each other. By generating SNF7 mutations that severely affect endocytic trafficking, but leave the Rim pathway function intact, we show that the two functions of SNF7 can be separated genetically. We analysed in detail how the SNF7 mutations affect the interaction of Snf7 with its various binding partners. Although the interactions with proteins Rim13 and Rim20, necessary for the Rim-pathway-related functions, were not altered by the mutations, there was a strong effect on interactions with components of the ESCRT pathway. The interactions, as measured by co-immunoprecipitation, with the ESCRT-III subunits Vps20 and Vps24 were strongly increased by the mutations, whereas the interactions with proteins Vps4 and Bro1, acting downstream of ESCRT-III, were reduced. As Vps4 is required for disassembly of ESCRT-III these results suggest that ESCRT-III is more stable in our SNF7 mutants. In line with this notion, a higher fraction of mutant Snf7 protein was detected at the membrane. Upon a shift to alkaline pH, a stronger binding signal for virtually all interaction partners, except Vps4, was observed. This indicates that the ESCRT network at the endosomal membrane is more extensive under these conditions.

Increasing Mitochondrial Membrane Phospholipid Content Lowers the Enzymatic Activity of Electron Transport Complexes

Biochemistry ◽  
2014 ◽  
Vol 53 (35) ◽  
pp. 5589-5591 ◽  
Author(s):  
Saame Raza Shaikh ◽  
E. Madison Sullivan ◽  
Rick J. Alleman ◽  
David A. Brown ◽  
Tonya N. Zeczycki
Keyword(s):  
Electron Transport ◽  
Enzymatic Activity ◽  
Mitochondrial Membrane ◽  
Membrane Phospholipid ◽  
Phospholipid Content ◽  
Electron Transport Complexes

Structure of contact sites between the outer and inner mitochondrial membranes investigated by HVEM tomography

1996 ◽  
Vol 54 ◽  
pp. 966-967
Author(s):  
C.A. Mannella ◽  
K.F. Buttle ◽  
K.A. O‘Farrell ◽  
A. Leith ◽  
M. Marko
Keyword(s):  
Liver Mitochondrion ◽  
Adenine Nucleotide ◽  
Protein Complexes ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Contact Sites ◽  
Transmission Electron ◽  
Precursor Proteins ◽  
Membrane Contacts ◽  
And Function

Early transmission electron microscopy of plastic-embedded, thin-sectioned mitochondria indicated that there are numerous junctions between the outer and inner membranes of this organelle. More recent studies have suggested that the mitochondrial membrane contacts may be the site of protein complexes engaged in specialized functions, e.g., import of mitochondrial precursor proteins, adenine nucleotide channeling, and even intermembrane signalling. It has been suggested that the intermembrane contacts may be sites of membrane fusion involving non-bilayer lipid domains in the two membranes. However, despite growing interest in the nature and function of intramitochondrial contact sites, little is known about their structure.We are using electron microscopic tomography with the Albany HVEM to determine the internal organization of mitochondria. We have reconstructed a 0.6-μm section through an isolated, plasticembedded rat-liver mitochondrion by combining 123 projections collected by tilting (+/- 70°) around two perpendicular tilt axes. The resulting 3-D image has confirmed the basic inner-membrane organization inferred from lower-resolution reconstructions obtained from single-axis tomography.

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