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Membrane Deformation Switching of an Endocytic Protein by Membrane Electrostatic Charge and Packing

55 Pages Posted: 21 Oct 2019 Sneak Peek Status: Review Complete

See all articles by Kazuki Kida

Kazuki Kida

Nara Institute of Science and Technology - Division of Biological Science

Manabu Kitamata

Nara Institute of Science and Technology - Division of Biological Science

Kazutaka Ikeda

RIKEN Center for Integrative Medical Sciences - Laboratory for Metabolomics

Kazuhiro Takemura

Tokyo Institute of Technology - School of Life Science and Technology

Takehiko Inaba

Nara Institute of Science and Technology - Division of Biological Science

Yugo Hayashi

Nara Institute of Science and Technology - Division of Materials Science

Kyoko Hanawa-Suetsugu

Nara Institute of Science and Technology - Division of Biological Science

Hironari Kamikubo

Nara Institute of Science and Technology - Division of Materials Science

Akio Kitao

Tokyo Institute of Technology - School of Life Science and Technology

Makoto Arita

RIKEN Center for Integrative Medical Sciences - Laboratory for Metabolomics

Shiro Suetsugu

Nara Institute of Science and Technology - Division of Biological Science

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Abstract

Bin-Amphiphysin-Rvs (BAR) domain proteins, including endophilin, deform membrane into tubules or vesicles for cellular processes, including endocytosis. The endophilin BAR domain has amphipathic helices, and degrees of insertion of these helices by mutations or phosphorylation cause a switch between tubule and vesicle formation. However, the membrane phospholipid properties causing switching remains unclear. We examined membrane deformation by endophilin using liposomes from various sources, including the plasma membrane, and found that endophilin vesiculated plasma membrane-derived liposomes. Endophilin vesiculated the plasma membrane-inspired reconstituted liposomes, which contained a small amount of charged phospholipids that resulted in uneven binding of endophilin. In contrast, the increase of charged phospholipids including phosphatidylinositol 4,5-bisphosphate resulted in tubulation by the increased binding of endophilin. Either tubulation or vesiculation required certain packing defects by the unsaturated acyl chains of phospholipids. Therefore, endophilin binding to membrane based on membrane charge density was the switch between tubulation and vesiculation, suggesting the importance of charge density in membrane deformation.

Keywords: BAR domain, packing-defects, tubulation, vesiculation, charge density, endocytosis

Suggested Citation

Kida, Kazuki and Kitamata, Manabu and Ikeda, Kazutaka and Takemura, Kazuhiro and Inaba, Takehiko and Hayashi, Yugo and Hanawa-Suetsugu, Kyoko and Kamikubo, Hironari and Kitao, Akio and Arita, Makoto and Suetsugu, Shiro, Membrane Deformation Switching of an Endocytic Protein by Membrane Electrostatic Charge and Packing (October 17, 2019). CELL-REPORTS-D-19-03972. Available at SSRN: https://ssrn.com/abstract=3471315 or http://dx.doi.org/10.2139/ssrn.3471315
This is a paper under consideration at Cell Press and has not been peer-reviewed.

Kazuki Kida

Nara Institute of Science and Technology - Division of Biological Science

Japan

Manabu Kitamata

Nara Institute of Science and Technology - Division of Biological Science

Japan

Kazutaka Ikeda

RIKEN Center for Integrative Medical Sciences - Laboratory for Metabolomics

Japan

Kazuhiro Takemura

Tokyo Institute of Technology - School of Life Science and Technology

2-12-1 O-okayama, Meguro-ku
Tokyo 152-8550, 52-8552
Japan

Takehiko Inaba

Nara Institute of Science and Technology - Division of Biological Science

Japan

Yugo Hayashi

Nara Institute of Science and Technology - Division of Materials Science

Ikoma, 630-0192
Japan

Kyoko Hanawa-Suetsugu

Nara Institute of Science and Technology - Division of Biological Science

Japan

Hironari Kamikubo

Nara Institute of Science and Technology - Division of Materials Science

Ikoma, 630-0192
Japan

Akio Kitao

Tokyo Institute of Technology - School of Life Science and Technology

2-12-1 O-okayama, Meguro-ku
Tokyo 152-8550, 52-8552
Japan

Makoto Arita

RIKEN Center for Integrative Medical Sciences - Laboratory for Metabolomics

Japan

Shiro Suetsugu (Contact Author)

Nara Institute of Science and Technology - Division of Biological Science ( email )

Japan

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