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- Title
Phosphorylation of Ykt6 SNARE Domain Regulates Its Membrane Recruitment and Activity.
- Authors
Karuna M, Pradhipa; Witte, Leonie; Linnemannstoens, Karen; Choezom, Dolma; Danieli-Mackay, Adi; Honemann-Capito, Mona; Gross, Julia Christina
- Abstract
Sensitive factor attachment protein receptors (SNARE) proteins are important mediators of protein trafficking that regulate the membrane fusion of specific vesicle populations and their target organelles. The SNARE protein Ykt6 lacks a transmembrane domain and attaches to different organelle membranes. Mechanistically, Ykt6 activity is thought to be regulated by a conformational change from a closed cytosolic form to an open membrane-bound form, yet the mechanism that regulates this transition is unknown. We identified phosphorylation sites in the SNARE domain of Ykt6 that mediate Ykt6 membrane recruitment and are essential for cellular growth. Using proximity-dependent labeling and membrane fractionation, we found that phosphorylation regulates Ykt6 conversion from a closed to an open conformation. This conformational switch recruits Ykt6 to several organelle membranes, where it functionally regulates the trafficking of Wnt proteins and extracellular vesicle secretion in a concentration-dependent manner. We propose that phosphorylation of its SNARE domain leads to a conformational switch from a cytosolic, auto-inhibited Ykt6 to an active SNARE at different membranes.
- Subjects
SNARE proteins; VESICLES (Cytology); WNT proteins; PHOSPHORYLATION; PROTEIN receptors
- Publication
Biomolecules (2218-273X), 2020, Vol 10, Issue 11, p1560
- ISSN
2218-273X
- Publication type
Article
- DOI
10.3390/biom10111560