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Lipid-Membrane Binding, Bending, and Pinching

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.

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Lipid-Membrane Binding, Bending, and Pinching

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  1. Lipid-Membrane Binding, Bending, and Pinching

  2. 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

  3. Two motifs contained in Many of these lipid-binding proteins • The ENTH/ANTH domain the Epsin N-terminal homology/AP180 N-terminal homology domain • The BAR domain the Bin-amphiphysin-Rvs161/167p domain

  4. 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 and PM.

  5. The BAR domain • The function of the BAR domain: As a mebrane curvature–sensing module. This domain is present in many proteins with roles in membrane dynamics,including membrane tubulation and ruffling .

  6. N-BAR domain An unstructured amphipathic helix is present N-terminal to the BAR domain .

  7. The functions of the N-BAR domain containing proteins sense and induce membrane curvature, presumably toward vesicle formation and scission.

  8. Common membrane-tubulating proteins at the PM and TGN R

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  10. R .

  11. 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.

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