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RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway
- Source :
- Journal of cell science. 116(Pt 20)
- Publication Year :
- 2003
-
Abstract
- The small GTPase Rab5, which cycles between active (GTP-bound) and inactive (GDP-bound) states, plays essential roles in membrane budding and trafficking in the early endocytic pathway. However, the molecular mechanisms underlying the Rab5-regulated processes are not fully understood other than the targeting event to early endosomes. Here, we report a novel Rab5-binding protein, RIN3, that contains many functional domains shared with other RIN members and additional Pro-rich domains. RIN3 displays the same biochemical properties as RIN2, the stimulator and stabilizer of GTP-Rab5. In addition, RIN3 exhibits its unique intracellular localization. RIN3 expressed in HeLa cells localized to cytoplasmic vesicles and the RIN3-positive vesicles contained Rab5 but not the early endosomal marker EEA1. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 was also capable of interacting via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. Interestingly, cytoplasmic amphiphysin II was translocated into the RIN3- and Rab5-positive vesicles when co-expressed with RIN3. These results indicate that RIN3 biochemically characterized as the stimulator and stabilizer for GTP-Rab5 plays an important role in the transport pathway from plasma membrane to early endosomes.
- Subjects :
- Endosome
Endocytic cycle
Vesicular Transport Proteins
Nerve Tissue Proteins
Endosomes
Biology
Endocytosis
Membrane Fusion
SH3 domain
EEA1
Two-Hybrid System Techniques
Chlorocebus aethiops
Animals
Guanine Nucleotide Exchange Factors
Humans
Small GTPase
Cloning, Molecular
Cells, Cultured
rab5 GTP-Binding Proteins
Microscopy, Confocal
Vesicle
Cytoplasmic Vesicles
Membrane Proteins
Biological Transport
Cell Biology
Membrane budding
Cell biology
Protein Structure, Tertiary
COS Cells
Carrier Proteins
HeLa Cells
Protein Binding
Subjects
Details
- ISSN :
- 00219533
- Volume :
- 116
- Issue :
- Pt 20
- Database :
- OpenAIRE
- Journal :
- Journal of cell science
- Accession number :
- edsair.doi.dedup.....ea6aa16ce526a2d2423a79318b63e7ec