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.

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

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 Title

PLoS ONE

Volume

18

Issue

9

First Page

e0291977

ISSN

1932-6203

PubMed ID

37751424



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