@article{oai:nagasaki-u.repo.nii.ac.jp:00000161,
 author = {Ogawa, Kohei and Kadowaki, Tomoko and Tokuhisa, Mitsuko and Yamaguchi, Yu and Umeda, Masahiro and Tsukuba, Takayuki},
 issue = {1},
 journal = {Scientific Reports},
 month = {Nov},
 note = {Rab44 is a large Rab GTPase that contains an amino-terminal EF-hand domain, a coiled-coil domain, and a carboxyl-terminal Rab GTPase domain.However, the roles of the EF-hand and coiled-coil domains remain unclear. Here, we constructed various deletion and point mutants of human Rab44. When overexpressed in HeLa cells, the wild-type Rab44 (hWT) formed ring-like structures, and partially localised to lysosomes. The dominant negative mutant, hT847N, localised to lysosomes and the cytosol, while the constitutively active mutant, hQ892L, 
formed ring-like structures, and partially localised to the plasma membrane and nuclei. The hΔEF, hΔcoil, and h826-1021 mutants also 
formed ring-like structures; however, their localisation patterns differed from hWT. Analysis of live imaging with LysoTracker revealed that the size of LysoTracker-positive vesicles was altered by all other mutations than the hC1019A and hΔEF. Treatment with ionomycin, a Ca2+ ionophore, induced the translocation of hWT and hΔcoil into the plasma membrane and cytosol, but had no effect on the localisation of the hΔEF and h826-1021 mutants. Thus, the EF- hand domain is likely required for the partial translocation of Rab44 to the plasma 
membrane and cytosol following transient Ca2+ influx, and the coiled-coil domain appears to be important for localisation and organelle formation., Scientific Reports, 10(1), art.no.19149; 2020},
 title = {Role of the EF-hand and coiled-coil domains of human Rab44 in localisation and organelle formation},
 volume = {10},
 year = {2020}
}