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Vol. 12, Issue 6, 1843-1857, June 2001
*Departments of Medicine, Surgery, and Cellular Biology and
Anatomy, Institute of Molecular Medicine and Genetics, Medical College
of Georgia and the Augusta VA Medical Center, Augusta, Georgia 30912;
Myosin Va is associated with discrete vesicle populations in a
number of cell types, but little is known of the function of myosin Vb.
Yeast two-hybrid screening of a rabbit parietal cell cDNA library with
dominant active Rab11a (Rab11aS20V) identified myosin Vb as an
interacting protein for Rab11a, a marker for plasma membrane recycling
systems. The isolated clone, corresponding to the carboxyl terminal 60 kDa of the myosin Vb tail, interacted with all members of the Rab11
family (Rab11a, Rab11b, and Rab25). GFP-myosin Vb and endogenous myosin
Vb immunoreactivity codistributed with Rab11a in HeLa and Madin-Darby
canine kidney (MDCK) cells. As with Rab11a in MDCK cells, the myosin Vb
immunoreactivity was dispersed with nocodazole treatment and relocated
to the apical corners of cells with taxol treatment. A green
fluorescent protein (GFP)-myosin Vb tail chimera overexpressed in HeLa
cells retarded transferrin recycling and caused accumulation of
transferrin and the transferrin receptor in pericentrosomal vesicles.
Expression of the myosin Vb tail chimera in polarized MDCK cells stably
expressing the polymeric IgA receptor caused accumulation of
basolaterally endocytosed polymeric IgA and the polymeric IgA receptor
in the pericentrosomal region. The myosin Vb tail had no effects on
transferrin trafficking in polarized MDCK cells. The GFP-myosin Va tail
did not colocalize with Rab11a and had no effects on recycling system vesicle distribution in either HeLa or MDCK cells. The results indicate
myosin Vb is associated with the plasma membrane recycling system in
nonpolarized cells and the apical recycling system in polarized cells.
The dominant negative effects of the myosin Vb tail chimera
indicate that this unconventional myosin is required for transit out of
plasma membrane recycling systems.
McLaughlin Research Institute, Great Falls, Montana
59405; and §Institut für Allgemeine Zoologie und
Genetik, Westf. Wilhelms-Universitat, Muenster, Germany
These authors contributed equally to this work.
Corresponding author. E-mail address:
jgolden{at}mail.mcg.edu.
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A. J. Lindsay, A. G. Hendrick, G. Cantalupo, F. Senic-Matuglia, B. Goud, C. Bucci, and M. W. McCaffrey Rab Coupling Protein (RCP), a Novel Rab4 and Rab11 Effector Protein J. Biol. Chem., March 29, 2002; 277(14): 12190 - 12199. [Abstract] [Full Text] [PDF]
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M. Fukuda, T. S. Kuroda, and K. Mikoshiba Slac2-a/Melanophilin, the Missing Link between Rab27 and Myosin Va. IMPLICATIONS OF A TRIPARTITE PROTEIN COMPLEX FOR MELANOSOME TRANSPORT J. Biol. Chem., March 29, 2002; 277(14): 12432 - 12436. [Abstract] [Full Text] [PDF]
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 J. C. S. Bizario, F. A. Castro, J. F. Sousa, R. N. Fernandes, A. D. Damiao, M. K. Oliveira, P. V. B. Palma, R. E. Larson, J. C. Voltarelli, and E. M. Espreafico Myosin-V colocalizes with MHC class II in blood mononuclear cells and is up-regulated by T-lymphocyte activation J. Leukoc. Biol., February 1, 2002; 71(2): 195 - 204. [Abstract] [Full Text] [PDF]
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O. C. Rodriguez and R. E. Cheney Human myosin-Vc is a novel class V myosin expressed in epithelial cells J. Cell Sci., January 3, 2002; 115(5): 991 - 1004. [Abstract] [Full Text] [PDF]
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R. Prekeris, J. M. Davies, and R. H. Scheller Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins J. Biol. Chem., October 12, 2001; 276(42): 38966 - 38970. [Abstract] [Full Text] [PDF]
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C. M. Hales, R. Griner, K. C. Hobdy-Henderson, M. C. Dorn, D. Hardy, R. Kumar, J. Navarre, E. K. L. Chan, L. A. Lapierre, and J. R. Goldenring Identification and Characterization of a Family of Rab11-interacting Proteins J. Biol. Chem., October 12, 2001; 276(42): 39067 - 39075. [Abstract] [Full Text] [PDF]
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J. A. Frazier, M. L. Wong, M. S. Longtine, J. R. Pringle, M. Mann, T. J. Mitchison, and C. Field Polymerization of Purified Yeast Septins: Evidence That Organized Filament Arrays May Not Be Required for Septin Function J. Cell Biol., November 2, 1998; 143(3): 737 - 749. [Abstract] [Full Text] [PDF]
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