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Updated: Jul 17, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Decoding ubiquitin sorting signals for clathrin-dependent endocytosis by CLASPs
Linton M Traub1, Gergely L Lukacs
1Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, PA 15261, USA, and Program in Cell and Lung Biology, Hospital for Sick Children Research Institute, Toronto, Ontario, Canada. traub@pitt.edu
Clathrin-mediated endocytosis uses diverse sorting signals, including ubiquitin, recognized by clathrin-coat-associated sorting proteins (CLASPs). This ensures specific cargo incorporation into vesicles, separating endocytosis from proteasomal degradation.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Clathrin-mediated endocytosis (CME) is crucial for cellular uptake.
- Cargo selectivity in CME is mediated by internalization signals.
- The adaptor protein AP-2 recognizes a limited set of these signals.
Purpose of the Study:
- To elucidate the molecular mechanisms behind the recognition of diverse endocytic signals by CME machinery.
- To investigate the role of ubiquitin as an internalization signal.
- To understand the function of clathrin-coat-associated sorting proteins (CLASPs).
Main Methods:
- Analysis of protein-protein interactions.
- Biochemical assays for ubiquitin binding.
- Cellular imaging techniques to observe cargo trafficking.
Main Results:
- Identified novel internalization signals, including ubiquitin, recognized by CLASPs.
- Demonstrated that CLASPs utilize ubiquitin-recognition modules similar to those in the 26S proteasome.
- Showed that ubiquitylated cargo is recruited to clathrin-coated pits during endocytosis.
Conclusions:
- CLASPs expand the repertoire of recognized endocytic signals beyond AP-2.
- Ubiquitin acts as a key signal for cargo selection in CME.
- Temporal and spatial regulation prevents interference between endocytosis and proteasomal degradation.
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