TY - JOUR
T1 - Identification and Characterization of a Family of Rab11-interacting Proteins
AU - Hales, Chadwick M.
AU - Griner, Richard
AU - Hobdy-Henderson, Karen C.
AU - Dorn, Matthew C.
AU - Hardy, David
AU - Kumar, Ravindra
AU - Navarre, Jennifer
AU - Chan, Edward K.L.
AU - Lapierre, Lynne A.
AU - Goldenring, James R.
PY - 2001/10/19
Y1 - 2001/10/19
N2 - Rab11a is a small GTP-binding protein enriched in the pericentriolar plasma membrane recycling systems. We hypothesized that Rab11a-binding proteins exist as downstream effectors of its action. Here we define a family of four Rab11-interacting proteins: Rab11-Family Interacting Protein 1 (Rab11-FIP1), Rab11-Family Interacting Protein 2 (Rab11-FIP2), Rab11-Family Interacting Protein 3 (Rab11-FIP3), and pp75/Rip11. All four interacting proteins associated with wild type Rab11a and dominant active Rab11a (Rab11aS20V) as well as Rab11b and Rab25. Rab11-FIP2 also interacted with dominant negative Rab11a (Rab11aS25N) and the tail of myosin Vb. The binding of Rab11-FIP1, Rab11-FIP2, and Rab11-FIP3 to Rab11a was dependent upon a conserved carboxyl-terminal amphipathic α-helix. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 colocalized with Rab11a in plasma membrane recycling systems in both non-polarized HeLa cells and polarized Madin-Darby canine kidney cells. GFP-Rab11-FIP3 also colocalized with Rab11a in HeLa cells. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 also coenriched with Rablla and H+K +-ATPase on parietal cell tubulovesicles, and Rab11-FIP1 and Rab11-FIP2 translocated with Rablla and the H+K+-ATPase upon stimulating parietal cells with histamine. The results suggest that the function of Rablla in plasma membrane recycling systems is dependent upon a compendium of protein effectors.
AB - Rab11a is a small GTP-binding protein enriched in the pericentriolar plasma membrane recycling systems. We hypothesized that Rab11a-binding proteins exist as downstream effectors of its action. Here we define a family of four Rab11-interacting proteins: Rab11-Family Interacting Protein 1 (Rab11-FIP1), Rab11-Family Interacting Protein 2 (Rab11-FIP2), Rab11-Family Interacting Protein 3 (Rab11-FIP3), and pp75/Rip11. All four interacting proteins associated with wild type Rab11a and dominant active Rab11a (Rab11aS20V) as well as Rab11b and Rab25. Rab11-FIP2 also interacted with dominant negative Rab11a (Rab11aS25N) and the tail of myosin Vb. The binding of Rab11-FIP1, Rab11-FIP2, and Rab11-FIP3 to Rab11a was dependent upon a conserved carboxyl-terminal amphipathic α-helix. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 colocalized with Rab11a in plasma membrane recycling systems in both non-polarized HeLa cells and polarized Madin-Darby canine kidney cells. GFP-Rab11-FIP3 also colocalized with Rab11a in HeLa cells. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 also coenriched with Rablla and H+K +-ATPase on parietal cell tubulovesicles, and Rab11-FIP1 and Rab11-FIP2 translocated with Rablla and the H+K+-ATPase upon stimulating parietal cells with histamine. The results suggest that the function of Rablla in plasma membrane recycling systems is dependent upon a compendium of protein effectors.
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U2 - 10.1074/jbc.M104831200
DO - 10.1074/jbc.M104831200
M3 - Article
C2 - 11495908
AN - SCOPUS:0035914343
SN - 0021-9258
VL - 276
SP - 39067
EP - 39075
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -