Phosphorylation of small GTPase Rab proteins from Bombyx mori (Lepidoptera: Bombycidae)

Title:

Phosphorylation of small GTPase Rab proteins from Bombyx mori (Lepidoptera: Bombycidae)

Creator:

Uno, Tomohide, Hata, Keisuke, Dieu Trang , Le Thi , Hiragaki, Susumu , Nakada, Takuya, Nakamura, Masahiko, Uno, Yuichi, Yamagata, Hiroshi, Kanamaru, Kengo , Takeda, Makio, and Matsubara, Mamoru

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:67b12548-cbfc-4b42-aaf0-120520269bde
uuid:67b12548-cbfc-4b42-aaf0-120520269bde

Subject:

Small GTP binding protein, Rab, Bombyx mori, PKC, and PTTH

Type:

article, model:article, and TEXT

Description:

Small GTPases of the Rab family act as essential regulators of vesicle transport pathways. Five Rab cDNA clones (BRab1, 7, 8, 11 and 14) from Bombyx mori were expressed in Escherichia coli as a thioredxin or glutathione sulfotransferase fusion protein. After purification, the fusion protein was tested for phosphorylation using protein kinase C (PKC). Results indicate that all of them were phosphorylated in vitro. The phosphorylation site of BRab1 was determined by mass-spectrometric analysis, which identified that Ser-17 of BRab1 was phosphorylated by PKC. Deletion and site-directed mutagenesis indicated that Ser-111of BRab8, in addition to Ser-17, was newly phosphorylated. Further immunohistochemical analysis using antibodies against Rab8 indicated that there are some Rab8 immunoreactive cells close to the neuropeptide secreting cells. This result suggests that in insects Rab proteins are regulated by phosphorylation and at least some of them are involved in neuropeptide secretion.

Language:

English

Rights:

http://creativecommons.org/publicdomain/mark/1.0/
policy:public

Source:

European Journal of Entomology | 2009 Volume:106 | Number:4

Harvested from:

CDK

Metadata only:

false