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This study explores the overlapping roles of lipid-binding scaffold proteins and lipid-modifying enzymes at the plasma membrane (PM) and trans-Golgi network (TGN). It highlights the redundancy in vesiculation machinery and the significance of motifs such as the ENTH/ANTH domains and BAR domains. These proteins are crucial for membrane bending and pinching, facilitating processes like clathrin-mediated endocytosis and cargo vesiculation. The report emphasizes how N-BAR domain proteins induce membrane curvature, contributing to the dynamics of vesicle formation from both PM and TGN.
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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
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
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.
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 .
N-BAR domain An unstructured amphipathic helix is present N-terminal to the BAR domain .
The functions of the N-BAR domain containing proteins sense and induce membrane curvature, presumably toward vesicle formation and scission.
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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.