Journal
CELLS & DEVELOPMENT
Volume 168, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.cdev.2021.203714
Keywords
Clathrin-mediated endocytosis; Clathrin adaptors; Membrane traffic; Protein self-assembly; Membrane biophysics
Categories
Funding
- Wellcome Trust Investigator Award [107858/Z/15/Z]
- Wellcome Trust PhD studentship of the Interdisciplinary Programme in Structural, Computational and Chemical Biology [102394/Z/13/Z]
- Wellcome Trust [102394/Z/13/Z, 107858/Z/15/Z] Funding Source: Wellcome Trust
Ask authors/readers for more resources
The AP2 adaptor complex plays a central role in regulating clathrin-mediated endocytosis, serving as a key hub for protein interactions beyond cargo recognition and clathrin recruitment. It mediates clathrin coated pit maturation and couples lattice formation to membrane deformation. AP2 complements the attenuating role of clathrin light chain subunits in driving clathrin assembly and dynamic lattice rearrangement for budding.
Orchestration of a complex network of protein interactions drives clathrin-mediated endocytosis (CME). A central role for the AP2 adaptor complex beyond cargo recognition and clathrin recruitment has emerged in recent years. It is now apparent that AP2 serves as a pivotal hub for protein interactions to mediate clathrin coated pit maturation, and couples lattice formation to membrane deformation. As a key driver for clathrin assembly, AP2 complements the attenuating role of clathrin light chain subunits, which enable dynamic lattice rearrangement needed for budding. This review summarises recent insights into AP2 function with respect to CME dynamics and biophysics, and its relationship to the role of clathrin light chains in clathrin assembly.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
