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TitleSite-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateOct 2, 2017
AuthorsDonghyuk Shin / Wooju Na / Ji-Hyung Lee / Gyuhee Kim / Jiseok Baek / Seok Hee Park / Cheol Yong Choi / Sangho Lee /
PubMed AbstractRab GTPases, which are involved in intracellular trafficking pathways, have recently been reported to be ubiquitinated. However, the functions of ubiquitinated Rab proteins remain unexplored. Here we ...Rab GTPases, which are involved in intracellular trafficking pathways, have recently been reported to be ubiquitinated. However, the functions of ubiquitinated Rab proteins remain unexplored. Here we show that Rab5 is monoubiquitinated on K116, K140, and K165. Upon co-transfection with ubiquitin, Rab5 exhibited abnormalities in endosomal localization and EGF-induced EGF receptor degradation. Rab5 K140R and K165R mutants restored these abnormalities, whereas K116R did not. We derived structural models of individual monoubiquitinated Rab5 proteins (mUbRab5s) by solution scattering and observed different conformational flexibilities in a site-specific manner. Structural analysis combined with biochemical data revealed that interactions with downstream effectors were impeded in mUbRab5, whereas GDP release and GTP loading activities were altered in mUbRab5. By contrast, mUbRab5 apparently had no effect. We propose a regulatory mechanism of Rab5 where monoubiquitination downregulates effector recruitment and GDP/GTP conversion in a site-specific manner.
External linksElife / PubMed:28968219 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDCM6:
Small GTPase Rab5 conjugated with ubiquitin at K116
Method: SAXS/SANS

SASDCN6:
Small GTPase Rab5 conjugated with ubiquitin at K140
Method: SAXS/SANS

SASDCP6:
Small GTPase Rab5 conjugated with ubiquitin at K165
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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