Journal
JOURNAL OF CELL SCIENCE
Volume 128, Issue 15, Pages 2781-2794Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.158634
Keywords
NAPG; STX7; STX8; Syntaxin 8; Endocytosis
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [23570174, 24790425, 25840042, 25291029]
- Grants-in-Aid for Scientific Research [26440105, 15K18507, 23570174, 24790425, 25840042] Funding Source: KAKEN
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Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) that reside in the target membranes and transport vesicles assemble into specific SNARE complexes to drive membrane fusion. N-ethylmaleimide-sensitive factor (NSF) and its attachment protein, alpha-SNAP (encoded by NAPA), catalyze disassembly of the SNARE complexes in the secretory and endocytic pathways to recycle them for the next round of fusion events. gamma-SNAP (encoded by NAPG) is a SNAP isoform, but its function in SNARE-mediated membrane trafficking remains unknown. Here, we show that gamma-SNAP regulates the endosomal trafficking of epidermal growth factor (EGF) receptor (EGFR) and transferrin. Immunoprecipitation and mass spectrometry analyses revealed that gamma-SNAP interacts with a limited range of SNAREs, including endosomal ones. gamma-SNAP, as well as alpha-SNAP, mediated the disassembly of endosomal syntaxin-7-containing SNARE complexes. Overexpression and small interfering (si) RNA-mediated depletion of gamma-SNAP changed the morphologies and intracellular distributions of endosomes. Moreover, the depletion partially suppressed the exit of EGFR and transferrin from EEA1-positive early endosomes to delay their degradation and uptake. Taken together, our findings suggest that gamma-SNAP is a unique SNAP that functions in a limited range of organelles - including endosomes and their trafficking pathways.
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