Next Article in Journal
Emerging Concepts of Hybrid Epithelial-to-Mesenchymal Transition in Cancer Progression
Previous Article in Journal
Ubiquitination of Intramitochondrial Proteins: Implications for Metabolic Adaptability
Open AccessArticle

Phosphorylation of Ykt6 SNARE Domain Regulates Its Membrane Recruitment and Activity

1
Hematology and Oncology, University Medical Center Goettingen, 37077 Goettingen, Germany
2
Developmental Biochemistry, University Medical Center Goettingen, 37077 Goettingen, Germany
3
HMU Health and Medical University Potsdam, 14471 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(11), 1560; https://doi.org/10.3390/biom10111560
Received: 16 October 2020 / Revised: 10 November 2020 / Accepted: 11 November 2020 / Published: 16 November 2020
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. View Full-Text
Keywords: Ykt6 conformational switch; membrane attachment; protein trafficking; secretory pathway Ykt6 conformational switch; membrane attachment; protein trafficking; secretory pathway
Show Figures

Figure 1

MDPI and ACS Style

Karuna M, P.; Witte, L.; Linnemannstoens, K.; Choezom, D.; Danieli-Mackay, A.; Honemann-Capito, M.; Gross, J.C. Phosphorylation of Ykt6 SNARE Domain Regulates Its Membrane Recruitment and Activity. Biomolecules 2020, 10, 1560.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop