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Guanine nucleotide exchange factor 2 for Rab5 proteins coordinated with GLUP6/GEF regulates the intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm.

Wen L, Fukuda M, Sunada M, Ishino S, Ishino Y, Okita TW, Ogawa M, Ueda T, Kumamaru T - J. Exp. Bot. (2015)

Bottom Line: Like GLUP6/GEF, Rab5-GEF2 was capable of activating Rab5a and two other Rab5 isoforms in in vitro GTP/GDP exchange assays.GEF proteins consist of the helical bundle (HB) domain at the N-terminus, Vps9 domain, and a C-terminal region.By the deletion analysis of GEFs, the HB domain was found essential for the activation of Rab5 proteins.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan Tobacco Research Institute, Chinese Academy of Agricultural Science, Qingdao 266101, China.

No MeSH data available.


Related in: MedlinePlus

Physical interactions of GLUP4/Rab5a with Rab5-GEF2 and GLUP6/GEF. Purified GLUP4/Rab5a was immobilized on Sensor Chip CM5, and various concentrations (1.5, 3.5, 5, 6.5, and 10.5 μM) of Rab5-GEF2 (A) and GLUP6/GEF (B) were loaded onto the chip for 120 s. Each sensorgram showed the actual binding responses obtained by subtraction of the background responses. Surface plasmon resonance analysis result showed that Rab5-GEF2 and GLUP6/GEF exhibited the same patterns of interaction with GLUP4/Rab5a.
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Figure 6: Physical interactions of GLUP4/Rab5a with Rab5-GEF2 and GLUP6/GEF. Purified GLUP4/Rab5a was immobilized on Sensor Chip CM5, and various concentrations (1.5, 3.5, 5, 6.5, and 10.5 μM) of Rab5-GEF2 (A) and GLUP6/GEF (B) were loaded onto the chip for 120 s. Each sensorgram showed the actual binding responses obtained by subtraction of the background responses. Surface plasmon resonance analysis result showed that Rab5-GEF2 and GLUP6/GEF exhibited the same patterns of interaction with GLUP4/Rab5a.

Mentions: In order to determine whether Rab5-GEF2 has the potential to activate GLUP4/Rab5a, we tested whether the two proteins physically interacted using surface plasmon resonance (SPR). The KD value of Rab5-GEF2 for GLUP4/Rab5a was measured at 1.7 μM, which is close to the KD (2.1 μM) observed for GLUP6/GEF. Moreover the overall response over time curves observed for the Rab5-GEF2 experiment was similar to that seen when GLUP6/GEF was used as the Rab5 activator (Fig. 6). This result indicates that Rab5-GEF2 physically interacts with GLUP4/Rab5a just as efficiently as with GLUP6/GEF.


Guanine nucleotide exchange factor 2 for Rab5 proteins coordinated with GLUP6/GEF regulates the intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm.

Wen L, Fukuda M, Sunada M, Ishino S, Ishino Y, Okita TW, Ogawa M, Ueda T, Kumamaru T - J. Exp. Bot. (2015)

Physical interactions of GLUP4/Rab5a with Rab5-GEF2 and GLUP6/GEF. Purified GLUP4/Rab5a was immobilized on Sensor Chip CM5, and various concentrations (1.5, 3.5, 5, 6.5, and 10.5 μM) of Rab5-GEF2 (A) and GLUP6/GEF (B) were loaded onto the chip for 120 s. Each sensorgram showed the actual binding responses obtained by subtraction of the background responses. Surface plasmon resonance analysis result showed that Rab5-GEF2 and GLUP6/GEF exhibited the same patterns of interaction with GLUP4/Rab5a.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4588877&req=5

Figure 6: Physical interactions of GLUP4/Rab5a with Rab5-GEF2 and GLUP6/GEF. Purified GLUP4/Rab5a was immobilized on Sensor Chip CM5, and various concentrations (1.5, 3.5, 5, 6.5, and 10.5 μM) of Rab5-GEF2 (A) and GLUP6/GEF (B) were loaded onto the chip for 120 s. Each sensorgram showed the actual binding responses obtained by subtraction of the background responses. Surface plasmon resonance analysis result showed that Rab5-GEF2 and GLUP6/GEF exhibited the same patterns of interaction with GLUP4/Rab5a.
Mentions: In order to determine whether Rab5-GEF2 has the potential to activate GLUP4/Rab5a, we tested whether the two proteins physically interacted using surface plasmon resonance (SPR). The KD value of Rab5-GEF2 for GLUP4/Rab5a was measured at 1.7 μM, which is close to the KD (2.1 μM) observed for GLUP6/GEF. Moreover the overall response over time curves observed for the Rab5-GEF2 experiment was similar to that seen when GLUP6/GEF was used as the Rab5 activator (Fig. 6). This result indicates that Rab5-GEF2 physically interacts with GLUP4/Rab5a just as efficiently as with GLUP6/GEF.

Bottom Line: Like GLUP6/GEF, Rab5-GEF2 was capable of activating Rab5a and two other Rab5 isoforms in in vitro GTP/GDP exchange assays.GEF proteins consist of the helical bundle (HB) domain at the N-terminus, Vps9 domain, and a C-terminal region.By the deletion analysis of GEFs, the HB domain was found essential for the activation of Rab5 proteins.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan Tobacco Research Institute, Chinese Academy of Agricultural Science, Qingdao 266101, China.

No MeSH data available.


Related in: MedlinePlus