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J. Cell Biol.,
Volume 142, Number 4, August 24, 1998 1023-1034
Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104
Dynactin, a multisubunit complex that binds
to the microtubule motor cytoplasmic dynein, may provide a link between dynein and its cargo. Many subunits of dynactin have been characterized, elucidating
the multifunctional nature of this complex. Using a dynein affinity column, p22, the smallest dynactin subunit, was isolated and microsequenced. The peptide sequences were used to clone a full-length human cDNA.
Database searches with the predicted amino acid sequence of p22 indicate that this polypeptide is novel.
We have characterized p22 as an integral component of dynactin by biochemical and immunocytochemical
methods. Affinity chromatography experiments indicate that p22 binds directly to the p150Glued subunit of
dynactin. Immunocytochemistry with antibodies to p22 demonstrates that this polypeptide localizes to punctate
cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles
throughout mitosis. Antibodies to p22, as well as to
other dynactin subunits, also revealed a novel localization for dynactin to the cleavage furrow and to the midbodies of dividing cells; cytoplasmic dynein was also localized to these structures. We therefore propose that
dynein/dynactin complexes may have a novel function
during cytokinesis.
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