Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, to early endocytic vesicles. Yoshikawa, M., Kajiho, H., Sakurai, K., Minoda, T., Nakagawa, S., Kontani, K., & Katada, T. Biochemical and Biophysical Research Communications, 372(1):168-172, Academic Press, 7, 2008.
abstract   bibtex   
The small GTPase Rab5 plays a key role in early endocytic pathway, and its activation requires guanine-nucleotide exchange factors (GEFs). Rab5-GEFs share a conserved VPS9 domain for the GEF action, and RIN3 containing additional domains, such as Src-homology 2, RIN-family homology (RH), and Ras-association (RA), was identified as a new Rab5-GEF. However, precise functions of the additional domains and the activation mechanism of RIN3 remain unknown. Here, we found tyrosine-phosphorylation signals are involved in the Rab5-GEF activation. Treatment of HeLa cells with pervanadate translocates RIN3 from cytoplasm to the Rab5-positive vesicles. This RIN3 translocation was applied to various mutants lacking each domain of RIN3. Our present results suggest that a Ras GTPase(s) activated by tyrosine-phosphorylation signals interacts with the inhibitory RA domain, resulting in an active conformation of RIN3 as a Rab5-GEF and that RIN-unique RH domain constitutes a Rab5-binding region for the progress of GEF action. © 2008 Elsevier Inc. All rights reserved.
@article{
 title = {Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, to early endocytic vesicles},
 type = {article},
 year = {2008},
 identifiers = {[object Object]},
 keywords = {Guanine-nucleotide exchange factor (GEF),Membrane traffic,RA domain,RH domain,RIN,Rab5,VPS9 domain},
 pages = {168-172},
 volume = {372},
 month = {7},
 publisher = {Academic Press},
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 abstract = {The small GTPase Rab5 plays a key role in early endocytic pathway, and its activation requires guanine-nucleotide exchange factors (GEFs). Rab5-GEFs share a conserved VPS9 domain for the GEF action, and RIN3 containing additional domains, such as Src-homology 2, RIN-family homology (RH), and Ras-association (RA), was identified as a new Rab5-GEF. However, precise functions of the additional domains and the activation mechanism of RIN3 remain unknown. Here, we found tyrosine-phosphorylation signals are involved in the Rab5-GEF activation. Treatment of HeLa cells with pervanadate translocates RIN3 from cytoplasm to the Rab5-positive vesicles. This RIN3 translocation was applied to various mutants lacking each domain of RIN3. Our present results suggest that a Ras GTPase(s) activated by tyrosine-phosphorylation signals interacts with the inhibitory RA domain, resulting in an active conformation of RIN3 as a Rab5-GEF and that RIN-unique RH domain constitutes a Rab5-binding region for the progress of GEF action. © 2008 Elsevier Inc. All rights reserved.},
 bibtype = {article},
 author = {Yoshikawa, Manabu and Kajiho, Hiroaki and Sakurai, Kyoko and Minoda, Tomohiro and Nakagawa, Satoshi and Kontani, Kenji and Katada, Toshiaki},
 journal = {Biochemical and Biophysical Research Communications},
 number = {1}
}

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