lipid-membrane binding, bending, and pinching
DESCRIPTION
Lipid-Membrane Binding, Bending, and Pinching. The same points of PM and TGN in my part. The vesiculation machinery is highly redundant at both sites . Many of the same types of lipid-binding scaffold proteins and classes of lipid-modifying enzymes are used at both sites. - PowerPoint PPT PresentationTRANSCRIPT
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Lipid-Membrane Binding, Bending, and Pinching
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The same points of PM and TGN in my part
The vesiculation machinery is highly redundant at both sites .
Many of the same types of lipid-binding scaffold proteins and classes of lipid-modifying enzymes are used at both sites
![Page 5: Lipid-Membrane Binding, Bending, and Pinching](https://reader035.vdocuments.us/reader035/viewer/2022062805/56814e35550346895dbb9c8a/html5/thumbnails/5.jpg)
Two motifs contained in Many of these lipid-binding proteins
The ENTH/ANTH domain the Epsin N-terminal homology/AP180 N-ter
minal homology domain The BAR domain the Bin-amphiphysin-Rvs161/167p domain
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The functions of the ENTH/ANTH domain containing proteins
Deform membrane. Support clathrin-mediated endocytosis or involve in CCV formation at the TGN or TGN a
nd PM.
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The BAR domain
The function of the BAR domain: As a mebrane curvature–sensing module. This domain is present in many proteinswith roles in membrane dynamics,including membrane tubulation and ruffling .
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N-BAR domain
An unstructured amphipathic helix is present N-terminal to the BAR domain .
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The functions of the N-BAR domain containing proteins
sense and induce membrane curvature, presumably toward vesicle formation and scission.
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Common membrane-tubulating proteins at the PM and TGN R
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R
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R
.
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Conclusion
A series of related ENTH/ANTH and BAR domain–containing proteins has been superimposed on the clathrin-adaptor sorting machinery to initiate the tubulation and vesiculation of sequestered cargo from both the PM and the TGN.