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Kinesin‐2 is a Motor for Late Endosomes and Lysosomes
Author(s) -
Brown Christa L.,
Maier Kerstin C.,
Stauber Tobias,
Ginkel Laura M.,
Wordeman Linda,
Vernos Isabelle,
Schroer Trina A.
Publication year - 2005
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2005.00347.x
Subject(s) - endosome , kinesin , endocytic cycle , lysosome , microbiology and biotechnology , biology , microtubule , motor protein , organelle , dynein , molecular motor , endocytosis , biochemistry , cell , enzyme , intracellular
The bidirectional nature of late endosome/lysosome movement suggests involvement of at least two distinct motors, one minus‐end directed and one plus‐end directed. Previous work has identified dynein as the minus‐end‐directed motor for late endosome/lysosome localization and dynamics. Conventional kinesin (kinesin‐1) has been implicated in plus‐end‐directed late endosome/lysosome movement, but other kinesin family members may also be involved. Kinesin‐2 is known to drive the movement of pigment granules, a type of lysosomally derived organelle, and was recently found to be associated with purified late endosomes. To determine whether kinesin‐2 might also power endosome movement in non‐pigmented cells, we overexpressed dominant negative forms of the KIF3A motor subunit and KAP3 accessory subunit and knocked down KAP3 levels using RNAi. We found kinesin‐2 to be required for the normal steady‐state localization of late endosomes/lysosomes but not early endosomes or recycling endosomes. Despite the abnormal subcellular distribution of late endosomes/lysosomes, the uptake and trafficking of molecules through the conventional endocytic pathway appeared to be unaffected. The slow time–course of inhibition suggests that both kinesin‐2 itself and its attachment to membranes do not turn over quickly.