Investigation of F-BAR domain PACSIN proteins uncovers membrane tubulation function in cilia assembly and transport

Christine Insinna, Quanlong Lu, Isabella Teixeira, Adam Harned, Elizabeth M. Semler, Jim Stauffer, Valentin Magidson, Ajit Tiwari, Anne K. Kenworthy, Kedar Narayan and Christopher J. Westlake ()
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Christine Insinna: National Cancer Institute, National Institutes of Health
Quanlong Lu: National Cancer Institute, National Institutes of Health
Isabella Teixeira: National Cancer Institute, National Institutes of Health
Adam Harned: National Institutes of Health
Elizabeth M. Semler: National Cancer Institute, National Institutes of Health
Jim Stauffer: National Cancer Institute, National Institutes of Health
Valentin Magidson: National Cancer Institute, National Institutes of Health
Ajit Tiwari: Vanderbilt University School of Medicine
Anne K. Kenworthy: Vanderbilt University School of Medicine
Kedar Narayan: National Institutes of Health
Christopher J. Westlake: National Cancer Institute, National Institutes of Health

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract The intracellular ciliogenesis pathway requires membrane trafficking, fusion, and reorganization. Here, we demonstrate in human cells and zebrafish that the F-BAR domain containing proteins PACSIN1 and -2 play an essential role in ciliogenesis, similar to their binding partner and membrane reorganizer EHD1. In mature cilia, PACSINs and EHDs are dynamically localized to the ciliary pocket membrane (CPM) and transported away from this structure on membrane tubules along with proteins that exit the cilium. PACSINs function early in ciliogenesis at the ciliary vesicle (CV) stage to promote mother centriole to basal body transition. Remarkably, we show that PACSIN1 and EHD1 assemble membrane tubules from the developing intracellular cilium that attach to the plasma membrane, creating an extracellular membrane channel (EMC) to the outside of the cell.

Date: 2019
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DOI: 10.1038/s41467-018-08192-9

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