In:
Journal of Cell Science, The Company of Biologists
Abstract:
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, α-SNAP, catalyze disassembly of the SNARE complexes in the secretory and endocytic pathways to recycle them for the next round of the fusion event. γ-SNAP is an isoform of SNAP, but its function in SNARE-mediated membrane trafficking remains unknown. Here, we show that γ-SNAP regulates endosomal trafficking of epidermal growth factor receptor (EGFR) and transferrin. Immunoprecipitation and mass spectrometry revealed that γ-SNAP interacts with limited SNAREs including endosomal ones. γ-SNAP, as well as α-SNAP, mediated disassembly of endosomal syntaxin 7-containing SNARE complexes. Overexpression and small interfering RNA-mediated depletion of γ-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 γ-SNAP is a unique SNAP that functions in limited organelles including endosomes and their trafficking pathways.
Type of Medium:
Online Resource
ISSN:
1477-9137
,
0021-9533
Language:
English
Publisher:
The Company of Biologists
Publication Date:
2015
detail.hit.zdb_id:
219171-4
detail.hit.zdb_id:
1483099-1
SSG:
12
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