<i>S</i>-acylation of YKT61 modulates its unconventional participation in the formation of SNARE complexes in Arabidopsis

Ting Ma; Jun-Ru Tan; Jin-Yu Lu; Sha Li; Yan Zhang

doi:10.1016/j.jgg.2024.04.007

Volume 51 Issue 10

Oct. 2024

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Article Navigation > Journal of Genetics and Genomics > 2024 > 51(10): 1079-1088

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S-acylation of YKT61 modulates its unconventional participation in the formation of SNARE complexes in Arabidopsis

doi: 10.1016/j.jgg.2024.04.007

a. College of Life Sciences, Shandong Agricultural University, Tai'an, Shandong 271018, China;
b. Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300071, China

Funds:

This work is supported by National Natural Science Foundation of China (31970332).

Received Date: 2024-02-02
Accepted Date: 2024-04-13
Rev Recd Date: 2024-04-11

Available Online: 2025-06-06

Publish Date: 2024-04-19

Abstract

Abstract

Hetero-tetrameric soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) complexes are critical for vesicle-target membrane fusion within the endomembrane system of eukaryotic cells. SNARE assembly involves four different SNARE motifs, Qa, Qb, Qc, and R, provided by three or four SNARE proteins. YKT6 is an atypical R-SNARE that lacks a transmembrane domain and is involved in multiple vesicle-target membrane fusions. Although YKT6 is evolutionarily conserved and essential, its function and regulation in different phyla seem distinct. Arabidopsis YKT61, the yeast and metazoan YKT6 homologue, is essential for gametophytic development, plays a critical role in sporophytic cells, and mediates multiple vesicle-target membrane fusion. However, its molecular regulation is unclear. We report here that YKT61 is S-acylated. Abolishing its S-acylation by a C195S mutation dissociates YKT61 from endomembrane structures and causes its functional loss. Although interacting with various SNARE proteins, YKT61 functions not as a canonical R-SNARE but coordinates with other R-SNAREs to participate in the formation of SNARE complexes. Phylum-specific molecular regulation of YKT6 may be evolved to allow more efficient SNARE assembly in different eukaryotic cells.
- Longin domain,
- S-acylation,
- Vesicle trafficking,
- R-SNARE,
- Arabidopsis thaliana

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