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Peer-reviewedCC BYTraffic (Copenhagen, Denmark)

Complexity of Clathrin Coat Dynamics in Endocytosis.

  • Anne-Laure Boinet1
  • Aurélien Roux1
  • Marko Kaksonen1
  1. 1Department of Biochemistry, University of Geneva, Geneva, Switzerland.
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Abstract

Clathrin-mediated endocytosis is a process by which eukaryotic cells internalise a wide range of molecules such as signalling factors, nutrients and membrane proteins, via the formation of a plasma-membrane-derived vesicle. This complex mechanism involves a coordinated assembly of the scaffold protein clathrin and more than 50 other endocytic proteins at endocytic sites. Clathrin polymerises into sturdy supramolecular lattices, yet its assembly is highly dynamic and controlled by the DnaJ/Hsc70 uncoating machinery. Although clathrin turnover at endocytic sites was proposed early on to allow membrane deformation to occur, more recent studies have started hinting at possible regulatory functions. In this review, we summarise and discuss the key findings that have advanced our understanding of the role played by clathrin dynamics, hoping to shed light on the complex regulation of the endocytic process.

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Cite

BibTeXRIS
BibTeX
@article{boinet2026complexity,
  title = {{Complexity of Clathrin Coat Dynamics in Endocytosis.}},
  author = {Anne-Laure Boinet and Aurélien Roux and Marko Kaksonen},
  journal = {Traffic (Copenhagen, Denmark)},
  year = {2026},
  month = oct,
  doi = {10.1111/tra.70052},
  url = {https://europepmc.org/article/MED/42920360},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Complexity of Clathrin Coat Dynamics in Endocytosis.
AU  - Anne-Laure Boinet
AU  - Aurélien Roux
AU  - Marko Kaksonen
PY  - 2026
DA  - 2026/10/30
JO  - Traffic (Copenhagen, Denmark)
DO  - 10.1111/tra.70052
UR  - https://europepmc.org/article/MED/42920360
AB  - Clathrin-mediated endocytosis is a process by which eukaryotic cells internalise a wide range of molecules such as signalling factors, nutrients and membrane proteins, via the formation of a plasma-membrane-derived vesicle. This complex mechanism involves a coordinated assembly of the scaffold protein clathrin and more than 50 other endocytic proteins at endocytic sites. Clathrin polymerises into sturdy supramolecular lattices, yet its assembly is highly dynamic and controlled by the DnaJ/Hsc70 uncoating machinery. Although clathrin turnover at endocytic sites was proposed early on to allow membrane deformation to occur, more recent studies have started hinting at possible regulatory functions. In this review, we summarise and discuss the key findings that have advanced our understanding of the role played by clathrin dynamics, hoping to shed light on the complex regulation of the endocytic process.
SN  - 1398-9219
SN  - 1600-0854
ER  -