γ-SNAP stimulates disassembly of endosomal SNARE complexes and regulates endocytic trafficking pathways
| Autor: | Kaori Hosoi, Akitsugu Yamamoto, Ayaka Tanaka, Daisuke Okuzaki, Hiroki Inoue, Masato Tanaka, Mitsuo Tagaya, Yuka Matsuzaki, Kenichi Asano, Kohei Arasaki, Katsuko Tani, Yuichi Wakana, Kaoru Ichimura |
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| Rok vydání: | 2015 |
| Předmět: |
Immunoprecipitation
Endosome Endocytic cycle Vesicular Transport Proteins Endosomes Biology Endocytosis Membrane Fusion Epidermal growth factor Humans RNA Small Interfering NAPA integumentary system Qa-SNARE Proteins Cell Membrane Transferrin Lipid bilayer fusion Hep G2 Cells Cell Biology Cell biology Transport protein ErbB Receptors Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Protein Transport stomatognathic diseases nervous system RNA Interference Protein Binding |
| Zdroj: | Journal of Cell Science. |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.158634 |
| Popis: | 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 (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. γ-SNAP (encoded by NAPG) is a SNAP isoform, but its function in SNARE-mediated membrane trafficking remains unknown. Here, we show that γ-SNAP regulates the endosomal trafficking of epidermal growth factor (EGF) receptor (EGFR) and transferrin. Immunoprecipitation and mass spectrometry analyses revealed that γ-SNAP interacts with a limited range of SNAREs, including endosomal ones. γ-SNAP, as well as α-SNAP, mediated the disassembly of endosomal syntaxin-7-containing SNARE complexes. Overexpression and small interfering (si)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 a limited range of organelles - including endosomes - and their trafficking pathways. |
| Databáze: | OpenAIRE |
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