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From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | + | The formation of clathrin basket is not spontaneous, there are proteins necessary to able this shape. These proteins called adaptors proteins fixe themselves to the N-terminal (bêta)-propeller domain of clathrin heavy chain. Theremore, with these proteins there are arrestins and Hsc70 which associate to the N-terminal (bêta)-propeller demain of clathrin heavy chain. Then, this part of the chain links to another part of the heavy chain leg. This step causes the subdivision of the distal and proximal domains with a kind of flexible knee link between them. | |
</StructureSection> | </StructureSection> | ||
Revision as of 18:27, 10 January 2019
Contents |
Generalities
Clathrin is a 3 legged protein with 3 heavy chains and 3 light chains. It has a triskelion shape (A tryskelion consists of three bent limbs radiating from a centre) and can self-assembled into a polyhedral structure arround vesicles of eukaryotic cells. Triskelia can polymerize into cages or even flat lattice, depending on the ratio hexagon/pentagon. A tryskelion consists of three bent limbs radiating from a centre.
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Function
Communication beetween the different compartiments of eukaryotic cell and plasma membrane is allowed by vesicles, which convey molecules within the cytoplasm. Clathrin are involved in the formation of those vesicles in a process named clathrin mediated endocytosis. Clathrins form a skeleton around the vesicle once several protein are assembled. The coated vesicles like so formed will then lose their round protein skeleton after their departure from the initial compartment because the clathrin cage is dismantled. This phenomena proceeds through five stages: initiation, cargo selection, coat assembly, scission and uncoating. During the cargo selection and the initiation, clathrins polymerize into hexagons and pentagons. The ratio between these two shapes dependents of the cells' curve.
Relevance
Clathrins are shown as a active player in the recycling of synaptics vesicles, though they are essential to the good functionement of synaptic transmission. Moreover, this specificity has a major role in signalling, in the motility of cell, in the communication between two cells and cells fate.
Structural highlights
The formation of clathrin basket is not spontaneous, there are proteins necessary to able this shape. These proteins called adaptors proteins fixe themselves to the N-terminal (bêta)-propeller domain of clathrin heavy chain. Theremore, with these proteins there are arrestins and Hsc70 which associate to the N-terminal (bêta)-propeller demain of clathrin heavy chain. Then, this part of the chain links to another part of the heavy chain leg. This step causes the subdivision of the distal and proximal domains with a kind of flexible knee link between them.
</StructureSection>
References
Molecular mechanism and physiological functions of clathrin‑mediated endocytosisVOLUME 12 | AUGUST 2011 Harvey T. McMahon and Emmanuel Boucrot VOLUME 12 | AUGUST 2011
