The Hob proteins are novel and conserved lipid-binding proteins at ER–PM contact sites

Author:

Neuman Sarah D.1,Jorgensen Jeff R.2,Cavanagh Amy T.1,Smyth Jeremy T.3ORCID,Selegue Jane E.1,Emr Scott D.2,Bashirullah Arash1ORCID

Affiliation:

1. Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705-2222, USA

2. Weill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA

3. Department of Anatomy, Physiology, and Genetics, F. Edward Hébert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814, USA

Abstract

ABSTRACT Membrane contact sites are critical junctures for organelle signaling and communication. Endoplasmic reticulum–plasma membrane (ER–PM) contact sites were the first membrane contact sites to be described; however, the protein composition and molecular function of these sites is still emerging. Here, we leverage yeast and Drosophila model systems to uncover a novel role for the Hobbit (Hob) proteins at ER–PM contact sites. We find that Hobbit localizes to ER–PM contact sites in both yeast cells and the Drosophila larval salivary glands, and this localization is mediated by an N-terminal ER membrane anchor and conserved C-terminal sequences. The C-terminus of Hobbit binds to plasma membrane phosphatidylinositols, and the distribution of these lipids is altered in hobbit mutant cells. Notably, the Hobbit protein is essential for viability in Drosophila, providing one of the first examples of a membrane contact site-localized lipid binding protein that is required for development.

Funder

National Institutes of Health

Cornell University

Publisher

The Company of Biologists

Subject

Cell Biology

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