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TBC1D9B functions as a GTPase-activating protein for Rab11a in polarized MDCK cells.

Gallo LI, Liao Y, Ruiz WG, Clayton DR, Li M, Liu YJ, Jiang Y, Fukuda M, Apodaca G, Yin XM - Mol. Biol. Cell (2014)

Bottom Line: In contrast, TBC1D9B had no effect on two Rab11a-independent pathways--basolateral recycling of the transferrin receptor or degradation of the epidermal growth factor receptor.Finally, expression of TBC1D9B decreased the amount of active Rab11a in the cell and concomitantly disrupted the interaction between Rab11a and its effector, Sec15A.We conclude that TBC1D9B is a Rab11a GAP that regulates basolateral-to-apical transcytosis in polarized MDCK cells.

View Article: PubMed Central - PubMed

Affiliation: Departments of Medicine, University of Pittsburgh, Pittsburgh, PA 15261.

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Domain structure of TBC1D9B and sequence comparisons of its TBC domain with other TBC domain–containing proteins. (A) Schematic of human TBC1D9B and Saccharomyces cerevisiae Gyp2p domain structure. Predicted GRAM domains are colored pink, TBC domains are colored green, and EF hands are colored light blue. (B) Alignment of the indicated region of the TBC domains using MAFFT software (Larkin et al., 2007; Katoh and Standley, 2013). Sequences including the arginine (R) and glutamine (Q) fingers are shaded gray; key amino acids in the R and Q fingers are shaded red. Identical residues are indicated with an asterisk, conserved amino acid substitutions by a colon, and semiconserved substitutions by a period. The percentage of identity (Id) or similarity (Sim) between the TBC domain of TBC1D9B and those of the indicated proteins is given in the right-hand columns.
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Figure 1: Domain structure of TBC1D9B and sequence comparisons of its TBC domain with other TBC domain–containing proteins. (A) Schematic of human TBC1D9B and Saccharomyces cerevisiae Gyp2p domain structure. Predicted GRAM domains are colored pink, TBC domains are colored green, and EF hands are colored light blue. (B) Alignment of the indicated region of the TBC domains using MAFFT software (Larkin et al., 2007; Katoh and Standley, 2013). Sequences including the arginine (R) and glutamine (Q) fingers are shaded gray; key amino acids in the R and Q fingers are shaded red. Identical residues are indicated with an asterisk, conserved amino acid substitutions by a colon, and semiconserved substitutions by a period. The percentage of identity (Id) or similarity (Sim) between the TBC domain of TBC1D9B and those of the indicated proteins is given in the right-hand columns.

Mentions: TBC1D9B is an ∼140-kDa TBC domain–containing protein with a comparable domain architecture to Gyp2p (Figure 1A). Furthermore, the overall similarity of these proteins is reasonably high at 49% and increases to 64% when the TBC domains are assessed individually. The TBC domain of TBC1D9B contains conserved R, Y, and Q residues, which form the “R” and “Q” fingers that are critical for GTP hydrolysis in other TBC proteins (Figure 1B; Pan et al., 2006; Gavriljuk et al., 2012).


TBC1D9B functions as a GTPase-activating protein for Rab11a in polarized MDCK cells.

Gallo LI, Liao Y, Ruiz WG, Clayton DR, Li M, Liu YJ, Jiang Y, Fukuda M, Apodaca G, Yin XM - Mol. Biol. Cell (2014)

Domain structure of TBC1D9B and sequence comparisons of its TBC domain with other TBC domain–containing proteins. (A) Schematic of human TBC1D9B and Saccharomyces cerevisiae Gyp2p domain structure. Predicted GRAM domains are colored pink, TBC domains are colored green, and EF hands are colored light blue. (B) Alignment of the indicated region of the TBC domains using MAFFT software (Larkin et al., 2007; Katoh and Standley, 2013). Sequences including the arginine (R) and glutamine (Q) fingers are shaded gray; key amino acids in the R and Q fingers are shaded red. Identical residues are indicated with an asterisk, conserved amino acid substitutions by a colon, and semiconserved substitutions by a period. The percentage of identity (Id) or similarity (Sim) between the TBC domain of TBC1D9B and those of the indicated proteins is given in the right-hand columns.
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Related In: Results  -  Collection

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Figure 1: Domain structure of TBC1D9B and sequence comparisons of its TBC domain with other TBC domain–containing proteins. (A) Schematic of human TBC1D9B and Saccharomyces cerevisiae Gyp2p domain structure. Predicted GRAM domains are colored pink, TBC domains are colored green, and EF hands are colored light blue. (B) Alignment of the indicated region of the TBC domains using MAFFT software (Larkin et al., 2007; Katoh and Standley, 2013). Sequences including the arginine (R) and glutamine (Q) fingers are shaded gray; key amino acids in the R and Q fingers are shaded red. Identical residues are indicated with an asterisk, conserved amino acid substitutions by a colon, and semiconserved substitutions by a period. The percentage of identity (Id) or similarity (Sim) between the TBC domain of TBC1D9B and those of the indicated proteins is given in the right-hand columns.
Mentions: TBC1D9B is an ∼140-kDa TBC domain–containing protein with a comparable domain architecture to Gyp2p (Figure 1A). Furthermore, the overall similarity of these proteins is reasonably high at 49% and increases to 64% when the TBC domains are assessed individually. The TBC domain of TBC1D9B contains conserved R, Y, and Q residues, which form the “R” and “Q” fingers that are critical for GTP hydrolysis in other TBC proteins (Figure 1B; Pan et al., 2006; Gavriljuk et al., 2012).

Bottom Line: In contrast, TBC1D9B had no effect on two Rab11a-independent pathways--basolateral recycling of the transferrin receptor or degradation of the epidermal growth factor receptor.Finally, expression of TBC1D9B decreased the amount of active Rab11a in the cell and concomitantly disrupted the interaction between Rab11a and its effector, Sec15A.We conclude that TBC1D9B is a Rab11a GAP that regulates basolateral-to-apical transcytosis in polarized MDCK cells.

View Article: PubMed Central - PubMed

Affiliation: Departments of Medicine, University of Pittsburgh, Pittsburgh, PA 15261.

Show MeSH