Identification and characterization of a novel variant in the highly conserved catalytic center of Rab11a

Small GTPases of the Rab family regulate vesicular traffic and distribution of proteins in different cell types. Rab11a is a member of this GTP hydrolyzing protein class and acts as a mediator of insulin stimulated translocation of the glucose transporter GLUT4 in peripheral tissues including heart and skeletal muscle. Here we report on Rab11a Q70R, a mutation in the catalytic center of Rab11a, observed in the cardiomyoblast cell line H9c2. Analysis of GTPase activity showed that Rab11a Q70L acts as a classical constitutive active mutant. Interestingly, the GTPase activity of Rab11a Q70R was not significantly different from the enzymatic activity of the Rab11a Q70 wild type protein. We therefore conclude that the glutamine residue of Rab11a at position 70 is not strictly essential for GTPase activity of this protein in contrast to Ras and other Rab proteins.