Abstract 2115 Phosphorylation of Serine Residues Impacts StarD6 Ligand-Binding Interactions

Phosphorylation is a post-translational modification that may regulate protein folding and more importantly, protein function. Moreover, phosphorylation may impact the amino acids in the binding site, contributing to its affinity towards certain ligands. StarD6 is a sterol binding protein, recognized as part of the StarD4 subfamily of the steroidogenic acute regulatory related lipid transfer (START) domain proteins. StarD6 was first discovered in testis germinal cells and is also expressed in the nervous system and brain regions such as the hippocampus.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109960
Primary Topic
Biochemical and Molecular Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 2115 Phosphorylation of Serine Residues Impacts StarD6 Ligand-Binding Interactions

Gabriella Papale, Brianna Getzoff
Journal of Biological Chemistry
Biochemical and Molecular Research
article

Abstract 2115 Phosphorylation of Serine Residues Impacts StarD6 Ligand-Binding Interactions

Gabriella Papale, Brianna Getzoff
article en

Abstract

Phosphorylation is a post-translational modification that may regulate protein folding and more importantly, protein function. Moreover, phosphorylation may impact the amino acids in the binding site, contributing to its affinity towards certain ligands. StarD6 is a sterol binding protein, recognized as part of the StarD4 subfamily of the steroidogenic acute regulatory related lipid transfer (START) domain proteins. StarD6 was first discovered in testis germinal cells and is also expressed in the nervous system and brain regions such as the hippocampus.

Journal of Biological ChemistryVol. 301(5)
Vassar College (US)
National Institutes of Health, National Institute of General Medical Sciences
Openalex Percentile: Top 88%
Biochemical and Molecular Research
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