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Vol. 12, Issue 7, 2195-2206, July 2001
and§
*Department of Foods and Nutrition, Kookmin University, 861-1, Chongnung-dong, Songbuk-gu, Seoul 136-702, Korea; Dynactin is a multisubunit complex that regulates the activities of
cytoplasmic dynein, a microtubule-associated motor. Actin-related protein 1 (Arp1) is the most abundant subunit of dynactin, and it forms
a short filament to which additional subunits associate. An Arp1
filament pointed-end-binding subcomplex has been identified that
consists of p62, p25, p27, and Arp11 subunits. The functional roles of
these subunits have not been determined. Recently, we reported the
cloning of an apparent homologue of mammalian Arp11 from the
filamentous fungus Neurospora crassa. Here, we report that N. crassa ro-2 and ro-12 genes
encode the respective p62 and p25 subunits of the pointed-end complex.
Characterization of School
of Biological Sciences, University of Missouri-Kansas City, Kansas
City, Missouri 64110-2499
ro-2, ro-7, and
ro-12 mutants reveals that each has a distinct phenotype. All three mutants have reduced in vivo vesicle trafficking and have defects in vacuole distribution. We showed previously that in
vivo dynactin function is required for high-level dynein ATPase
activity, and we find that all three mutants have low dynein ATPase
activity. Surprisingly, ro-12 differs from
ro-2 and ro-7 and other previously
characterized dynein/dynactin mutants in that it has normal nuclear
distribution. Each of the mutants shows a distinct dynein/dynactin
localization pattern. All three mutants also show stronger
dynein/dynactin-membrane interaction relative to wild type, suggesting
that the Arp1 pointed-end complex may regulate interaction of dynactin
with membranous cargoes.
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