Journal
JOURNAL OF PHYSIOLOGICAL SCIENCES
Volume 69, Issue 2, Pages 263-280Publisher
SPRINGER JAPAN KK
DOI: 10.1007/s12576-018-0644-2
Keywords
Class II PI3K; PI3K-C2 alpha; PI3K-C2 beta; Pinocytosis; Clathrin; Endothelial cell
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Funding
- Japan International Cooperation Agency (JICA) [J-14-10306]
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan [25116711]
- Japan Society for the Promotion of Science [17K08532, 16K18988, 16K15409, 17K08542, 15H04673]
- Grants-in-Aid for Scientific Research [15H04673, 16K18988, 17K08542, 25116711, 17K08532, 16K15409] Funding Source: KAKEN
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Pinocytosis is an important fundamental cellular process that is used by the cell to transport fluid and solutes. Phosphoinositide 3-kinases (PI3Ks) regulate a diverse array of dynamic membrane events. However, it is not well-understood which PI3K isoforms are involved in specific mechanisms of pinocytosis. We performed knockdown studies of endogenous PI3K isoforms and clathrin heavy chain (CHC)mediated by small interfering RNA (siRNA). The results demonstrated that the class II PI3K PI3K-C2 alpha and PI3K-C2 beta, but not the class I or III PI3K, were required for pinocytosis, based on an evaluation of fluorescein-5-isothiocyanate (FITC)-dextran uptake in endothelial cells. Pinocytosis was partially dependent on both clathrin and dynamin, and both PI3K-C2 alpha and PI3K-C2 beta were required for clathrin-mediatedbut not clathrin-non-mediatedFITC-dextran uptake at the step leading up to its delivery to early endosomes. Both PI3K-C2 alpha and PI3K-C2 beta were co-localized with clathrin-coated pits and vesicles. However, PI3K-C2, but not PI3K-C2, was highly co-localized with actin filament-associated clathrin-coated structures and required for actin filament formation at the clathrin-coated structures. These results indicate that PI3K-C2 alpha and PI3K-C2 beta play differential, indispensable roles in clathrin-mediated pinocytosis.
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