Ferreira, APA;
Boucrot, E;
(2018)
Mechanisms of Carrier Formation during Clathrin-Independent Endocytosis.
Trends in Cell Biology
, 28
(3)
pp. 188-200.
10.1016/j.tcb.2017.11.004.
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Abstract
Clathrin-independent endocytosis (CIE) mediates the cellular uptake of many extracellular ligands, receptors, and pathogens, including several life-threatening bacterial toxins and viruses. So far, our understanding of CIE carrier formation has lagged behind that of clathrin-coated vesicles. Impediments have been the imprecise definition of some CIE pathways, the lack of specific cargoes being transported and of exclusive cytosolic markers and regulators. Notwithstanding these limitations, three distinct molecular mechanisms by which CIE carriers form can be defined. Cargo capture by cytosolic proteins is the main mechanism used by fast endophilin-mediated endocytosis (FEME) and interleukin 2 receptor (IL-2R) endocytosis. Acute signaling-induced membrane remodeling drives macropinocytosis. Finally, extracellular lipid or cargo clustering by the glycolipid-lectin (GL-Lect) hypothesis mediates the uptake of Shiga and cholera toxins and receptors by the CLIC/GEEC pathway. Here, we review these mechanisms and highlight current gaps in knowledge that will need to be addressed to complete our understanding of CIE.
| Type: | Article |
|---|---|
| Title: | Mechanisms of Carrier Formation during Clathrin-Independent Endocytosis |
| Location: | England |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.tcb.2017.11.004 |
| Publisher version: | http://dx.doi.org/10.1016/j.tcb.2017.11.004 |
| Language: | English |
| Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
| Keywords: | Caveolae, clathrin-independent carriers/GPI-AP enriched endocytic compartments (CLIC/GEEC), clathrin-independent endocytosis, fast endophilin-mediated endocytosis (FEME), glycolipid-lectin (GL-Lect) hypothesis, glycosylphosphatidylinositol (GPI)-anchored proteins, macropinocytosis |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10044610 |
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