Dimerization properties of Rabaptin-5 and its isoforms.
Rabaptin-5 plays an important role in intracellular membrane traffic acting as an effector molecule of small GTPases Rab5 and Rab4. It was previously demonstrated that Rabaptin-5 exists as a part of a large protein complex in vivo and is able to form dimers in vitro. Data of X-ray structural analysis suggest that dimerization of Rabaptin-5 is an important feature required for its interaction with Rab5 GTPase. Recently several isoforms of Rabaptin-5 characterized by various deletions in the polypeptide chains have been identified. These isoforms might exhibit functional properties that differ from those of Rabaptin-5. In this study, we have investigated dimerization properties of delta and gamma isoforms of Rabaptin-5. In addition, we have provided the first direct evidence for Rabaptin-5 dimerization in cells.
Korobko
E V
EV
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Kiselev
S L
SL
Korobko
I V
IV
D001692:Biological Transport / Q000502:physiology; D002460:Cell Line; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D020798:Two-Hybrid System Techniques; D033921:Vesicular Transport Proteins / Q000235:genetics / Q000378:metabolism*; D020695:rab4 GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism; D020696:rab5 GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism
D020033:Protein Isoforms; C097227:RABEP1 protein, human; D033921:Vesicular Transport Proteins; D020695:rab4 GTP-Binding Proteins; D020696:rab5 GTP-Binding Proteins