Publication Date

9-26-2023

Document Type

Article

Organizational Units

College of Natural Science and Mathematics, Biological Sciences

Keywords

Large dense core vesicles, HID-1, Endocrine system, Neuropeptides, Peptides

Abstract

Large dense core vesicles (LDCVs) mediate the regulated release of neuropeptides and peptide hormones. HID-1 is a trans-Golgi network (TGN) localized peripheral membrane protein contributing to LDCV formation. There is no information about HID-1 structure or domain architecture, and thus it remains unknown how HID-1 binds to the TGN and performs its function. We report that the N-terminus of HID-1 mediates membrane binding through a myristoyl group with a polybasic amino acid patch but lacks specificity for the TGN. In addition, we show that the C-terminus serves as the functional domain. Indeed, this isolated domain, when tethered to the TGN, can rescue the neuroendocrine secretion and sorting defects observed in HID-1 KO cells. Finally, we report that a point mutation within that domain, identified in patients with endocrine and neurological deficits, leads to loss of function.

Copyright Date

9-26-2023

Copyright Statement / License for Reuse

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Rights Holder

Blake H. Hummer, Theodore Carter, Breanna L. Sellers, Jenna D. Triplett, and Cedric S. Asensio

Provenance

Received from Faculty Publications Booklet

File Format

application/pdf

Language

English (eng)

Extent

14 pgs

File Size

1.75 MB

Publication Statement

Copyright is held by the authors. User is responsible for all copyright compliance. This article was originally published as:

Hummer, B. H., Carter, T., Sellers, B. L., Triplett, J. D., & Asensio, C. S. (2023). Identification of the functional domain of the dense core vesicle biogenesis factor HID-1. PLOS ONE, 18(9), e0291977. https://doi.org/10.1371/journal.pone.0291977

Publication Title

PLoS ONE

Volume

18

Issue

9

First Page

e0291977

ISSN

1932-6203

PubMed ID

37751424



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