期刊
MOLECULAR PLANT
卷 1, 期 6, 页码 961-976出版社
CELL PRESS
DOI: 10.1093/mp/ssn057
关键词
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资金
- National Science Foundation [IOB-0515998]
- Iowa State University Plant Sciences Institute
Sorting nexins are conserved proteins that function in vesicular trafficking and contain a characteristic phox homology (PX) domain. Here, we characterize the ubiquitously expressed Arabidopsis thaliana sorting nexin AtSNX2b. Sub-cellular fractionation studies indicate that AtSNX2b is peripherally associated with membranes. The AtSNX2b PX domain binds to phosphatidylinositol 3-phosphate in vitro and this association is required for the localization of GFP-AtSNX2b to punctate structures in vivo, identified as the trans-Golgi network, prevacuolar compartment and endosomes. Overexpression of GFP-tagged AtSNX2b produces enlarged GFP-labeled compartments that can also be labeled by the endocytic tracer FM4-64. Endocytic trafficking of FM4-64 to the vacuole is arrested in these GFP-AtSNX2b compartments, and similar FM4-64-accumulating compartments are seen upon overexpression of untagged AtSNX2b. This suggests that exit of membrane components from these enlarged or aggregated endosomes is inhibited. Vacuolar proteins containing an N-terminal propeptide, but not those with a C-terminal propeptide, are also present in these enlarged compartments. We hypothesize that AtSNX2b is involved in vesicular trafficking from endosomes to the vacuole.
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