Lipid-Membrane Binding, Bending, and Pinching
Jan 19, 2016
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
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
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.
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 .
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.
Common membrane-tubulating proteins at the PM and TGN R
R
R
.
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.