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Vol. 13, Issue 3, 817-829, March 2002
Department of Molecular, Cellular, and Developmental Biology,
University of Colorado, Boulder, Colorado 80309-0347
The diversity of dynein's functions in mammalian cells is a
manifestation of both the existence of multiple dynein heavy chain isoforms and an extensive set of associated protein subunits. In this
study, we have identified and characterized a novel subunit of the
mammalian cytoplasmic dynein 2 complex. The sequence similarity between
this 33-kDa subunit and the light intermediate chains (LICs) of
cytoplasmic dynein 1 suggests that this protein is a dynein 2 LIC
(D2LIC). D2LIC contains a P-loop motif near its NH2 terminus, and it shares a short region of similarity to the yeast GTPases Spg1p and Tem1p. The D2LIC subunit interacts specifically with
DHC2 (or cDhc1b) in both reciprocal immunoprecipitations and
sedimentation assays. The expression of D2LIC also mirrors that of DHC2
in a variety of tissues. D2LIC colocalizes with DHC2 at the Golgi
apparatus throughout the cell cycle. On brefeldin A-induced Golgi
fragmentation, a fraction of D2LIC redistributes to the cytoplasm,
leaving behind a subset of D2LIC that is localized around the
centrosome. Our results suggest that D2LIC is a bona fide subunit of
cytoplasmic dynein 2 that may play a role in maintaining Golgi
organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.
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