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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Christine Insinna, Quanlong Lu, Isabella Teixeira, Adam Harned, Elizabeth M. Semler, Jim Stauffer, Valentin Magidson, Ajit Tiwari, Anne K. Kenworthy, Kedar Narayan, Christopher J. Westlake

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 t7ubules from the developing intracellular cilium that attach to the plasma membrane, creating an extracellular membrane channel (EMC) to the outside of the cell. Together, our work uncovers a function for F-BAR proteins and membrane tubulation in ciliogenesis and explains how the intracellular cilium emerges from the cell. More... »

PAGES

428

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-018-08192-9

DOI

http://dx.doi.org/10.1038/s41467-018-08192-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111655103

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30683896


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