Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 22, Issue 14, Pages 2579-2587Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-04-0279
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Funding
- Ministry of Education, Culture, Sports, Science and Technology
- Uehara Memorial Foundation
- Astellas Foundation for Research on Metabolic Disorders
- Japanese Ministry of Education, Culture, Sports, Science and Technology
- Institute for Molecular and Cellular Regulation
- Gunma University
- Grants-in-Aid for Scientific Research [21390050, 23687027] Funding Source: KAKEN
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It is generally accepted that soluble N-ethylmaleimide-sensitive factor attachment protein receptors mediate the docking and fusion of transport intermediates with target membranes. Our research identifies Caenorhabditis elegans homologue of synaptosomal-associated protein 29 (SNAP-29) as an essential regulator of membrane trafficking in polarized intestinal cells of living animals. We show that a depletion of SNAP-29 blocks yolk secretion and targeting of apical and basolateral plasma membrane proteins in the intestinal cells and results in a strong accumulation of small cargo-containing vesicles. The loss of SNAP-29 also blocks the transport of yolk receptor RME-2 to the plasma membrane in nonpolarized oocytes, indicating that its function is required in various cell types. SNAP-29 is essential for embryogenesis, animal growth, and viability. Functional fluorescent protein-tagged SNAP-29 mainly localizes to the plasma membrane and the late Golgi, although it also partially colocalizes with endosomal proteins. The loss of SNAP-29 leads to the vesiculation/fragmentation of the Golgi and endosomes, suggesting that SNAP-29 is involved in multiple transport pathways between the exocytic and endocytic organelles. These observations also suggest that organelles comprising the endomembrane system are highly dynamic structures based on the balance between membrane budding and fusion and that SNAP-29-mediated fusion is required to maintain proper organellar morphology and functions.
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