Abstract
Small GTPases of the Rab family are key regulators of membrane trafficking. Monoclonal antibodies are useful tools for identifying proteins that interact with other proteins and for examining their tissue distribution. We selected a monoclonal antibody against Rab8 of Bombyx mori L. It specifically recognized amino acid residues 30-109, which are conserved among Rab8 proteins, and did not recognize any other Rab proteins. Western blotting using the antibody revealed one band in the brains of B. mori and rat. Far-Western blotting analysis detected three proteins interacting with Rab8. These results indicate that this antibody is useful for clarifying the physiological function of Rab8 of B. mori and other species. This is a report of a study on a monoclonal antibody against insect Rab protein.
Highlights
The Rab proteins comprise the largest subgroup of the Ras superfamily of small GTPases, which includes almost 70 members
We carried out Western blotting (Fig. 1)
The band of 28 kDa might not be detected. These results suggest that proteins that interact with BRab8 occur in the brain of B. mori
Summary
The Rab proteins comprise the largest subgroup of the Ras superfamily of small GTPases, which includes almost 70 members. These proteins act as regulators of trafficking between subcellular compartments in eukaryotic cells (Zerial et al, 2001; Deneka et al, 2003). Conserved regions are involved in guanine and phosphate/magnesium binding (Pereira-Leal & Seabra, 2000). Like other GTPases, Rab proteins cycle between active GTP-bound and inactive GDP-bound forms. The GTP-bound form binds many effector proteins and carries out a variety of cellular processes (Jordens et al, 2005; Grosshans et al, 2006). After Rab proteins complete their designated function on the membrane, they return to the inactive GDP-bound form in the cytosol
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