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J. Biol. Chem., Vol. 275, Issue 41, 31798-31804, October 13, 2000
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From the School of Biological Sciences, University of Missouri,
Kansas City, Missouri 64110-2499
Cytoplasmic dynein is a microtubule-associated
motor that utilizes ATP hydrolysis to conduct minus-end directed
transport of various organelles. Dynactin is a multisubunit complex
that has been proposed to both link dynein with cargo and activate dynein motor function. The mechanisms by which dynactin regulates dynein activity are not clear. In this study, we examine the role of
dynactin in regulating dynein ATPase activity. We show that dynein-microtubule binding and ATP-dependent release of
dynein from microtubules are reduced in dynactin null mutants,
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF196291.
Cytoplasmic Dynein ATPase Activity Is Regulated by
Dynactin-dependent Phosphorylation*
, and
ro-3 (p150Glued) and ro-4
(Arp1), relative to wild-type. The dynein-microtubule binding activity,
but not the ATP-dependent release of dynein from
microtubules, is restored by in vitro mixing of extracts from dynein and dynactin mutants. Dynein produced in a
ro-3 mutant has ~8-fold reduced ATPase activity
relative to dynein isolated from wild-type. However, dynein ATPase
activity from wild-type is not reduced when dynactin is separated from
dynein, suggesting that dynein produced in a dynactin mutant is
inactivated. Treatment of dynein isolated from the ro-3
mutant with 
protein phosphatase restores the ATPase activity to
near wild-type levels. The reduced dynein ATPase activity observed in
dynactin null mutants is mainly due to altered affinity for ATP.
Radiolabeling experiments revealed that low molecular mass proteins,
particularly 20- and 8-kDa proteins, that immunoprecipitate with dynein
heavy chain are hyperphosphorylated in the dynactin mutant and
dephosphorylated upon protein phosphatase treatment. The results
suggest that cytoplasmic dynein ATPase activity is regulated by
dynactin-dependent phosphorylation of dynein light chains.
*
This work was supported by National Institutes of Health
Grant GM51217 (to M. P.)The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Biological Science, Myongji University,
Yongin, Kyunggi-do 449-728, Korea.
§
To whom correspondence should be addressed: School of Biological
Sciences, University of Missouri, 5100 Rockhill Rd., Kansas City, MO
64110-2499. Tel.: 816-235-2593; Fax: 816-235-1503; E-mail: plamannm@umkc.edu.
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